https://wiki.oroboros.at/api.php?action=feedcontributions&user=Plangger+Mario&feedformat=atomBioblast - User contributions [en]2024-03-28T21:13:37ZUser contributionsMediaWiki 1.36.1https://wiki.oroboros.at/index.php?title=Hunter-Manseau_2024_Insect_Sci&diff=246671Hunter-Manseau 2024 Insect Sci2024-03-27T14:53:28Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Hunter-Manseau F, Cormier SB, Strang R, Pichaud N (2024) Fasting as a precursor to high-fat diet enhances mitochondrial resilience in ''Drosophila melanogaster''. Insect Sci [Epub ahead of print]. https://doi.org/10.1111/1744-7917.13355<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38514255 PMID: 38514255 Open Access]<br />
|authors=Hunter-Manseau Florence, Cormier Simon B, Strang Rebekah, Pichaud Nicolas<br />
|year=2024<br />
|journal=Insect Sci<br />
|abstract=Changes in diet type and nutrient availability can impose significant environmental stress on organisms, potentially compromising physiological functions and reproductive success. In nature, dramatic fluctuations in dietary resources are often observed and adjustments to restore cellular homeostasis are crucial to survive this type of stress. In this study, we exposed male ''Drosophila melanogaster'' to two modulated dietary treatments: one without a fasting period before exposure to a high-fat diet and the other with a 24-h fasting period. We then investigated mitochondrial metabolism and molecular responses to these treatments. Exposure to a high-fat diet without a preceding fasting period resulted in disrupted mitochondrial respiration, notably at the level of complex I. On the other hand, a short fasting period before the high-fat diet maintained mitochondrial respiration. Generally, transcript abundance of genes associated with mitophagy, heat-shock proteins, mitochondrial biogenesis, and nutrient sensing pathways increased either slightly or significantly following a fasting period and remained stable when flies were subsequently put on a high-fat diet, whereas a drastic decrease of almost all transcript abundances was observed for all these pathways when flies were exposed directly to a high-fat diet. Moreover, mitochondrial enzymatic activities showed less variation after the fasting period than the treatment without a fasting period. Overall, our study sheds light on the mechanistic protective effects of fasting prior to a high-fat diet and highlights the metabolic flexibility of ''Drosophila'' mitochondria in response to abrupt dietary changes and have implication for adaptation of species to their changing environment.<br />
|keywords=Dietary modulation, Fasting, High‐fat diet, Metabolic flexibility, Mitochondrial metabolism, Stress response<br />
|editor=[[Plangger M]]<br />
|mipnetlab=CA Moncton Hebert-Chatelain E, CA Moncton Pichaud N<br />
}}<br />
{{Labeling<br />
|area=Respiration, Exercise physiology;nutrition;life style<br />
|organism=Drosophila<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Hunter-Manseau_2024_Insect_Sci&diff=246670Hunter-Manseau 2024 Insect Sci2024-03-27T14:33:44Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Hunter-Manseau F, Cormier SB, Strang R, Pichaud N (2024) Fasting as a precursor to high-fat diet enhances mitochondrial resilience in ''Drosophila melanogaster''. Insect Sci [Epub ahead of print]. https://doi.org/10.1111/1744-7917.13355<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38514255 PMID: 38514255 Open Access]<br />
|authors=Hunter-Manseau Florence, Cormier Simon B, Strang Rebekah, Pichaud Nicolas<br />
|year=2024<br />
|journal=Insect Sci<br />
|abstract=Changes in diet type and nutrient availability can impose significant environmental stress on organisms, potentially compromising physiological functions and reproductive success. In nature, dramatic fluctuations in dietary resources are often observed and adjustments to restore cellular homeostasis are crucial to survive this type of stress. In this study, we exposed male ''Drosophila melanogaster'' to two modulated dietary treatments: one without a fasting period before exposure to a high-fat diet and the other with a 24-h fasting period. We then investigated mitochondrial metabolism and molecular responses to these treatments. Exposure to a high-fat diet without a preceding fasting period resulted in disrupted mitochondrial respiration, notably at the level of complex I. On the other hand, a short fasting period before the high-fat diet maintained mitochondrial respiration. Generally, transcript abundance of genes associated with mitophagy, heat-shock proteins, mitochondrial biogenesis, and nutrient sensing pathways increased either slightly or significantly following a fasting period and remained stable when flies were subsequently put on a high-fat diet, whereas a drastic decrease of almost all transcript abundances was observed for all these pathways when flies were exposed directly to a high-fat diet. Moreover, mitochondrial enzymatic activities showed less variation after the fasting period than the treatment without a fasting period. Overall, our study sheds light on the mechanistic protective effects of fasting prior to a high-fat diet and highlights the metabolic flexibility of ''Drosophila'' mitochondria in response to abrupt dietary changes and have implication for adaptation of species to their changing environment.<br />
|keywords=Dietary modulation, Fasting, High‐fat diet, Metabolic flexibility, Mitochondrial metabolism, Stress response<br />
|editor=[[Plangger M]]<br />
|mipnetlab=CA Moncton Hebert-Chatelain E, CA Moncton Pichaud N<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Drosophila<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Insect_Sci&diff=246667Insect Sci2024-03-27T14:18:19Z<p>Plangger Mario: Created page with "{{Journal |Title=[https://onlinelibrary.wiley.com/journal/17447917 Insect Science] }}"</p>
<hr />
<div>{{Journal<br />
|Title=[https://onlinelibrary.wiley.com/journal/17447917 Insect Science]<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Hunter-Manseau_2024_Insect_Sci&diff=246666Hunter-Manseau 2024 Insect Sci2024-03-27T14:17:54Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Hunter-Manseau F, Cormier SB, Strang R, Pichaud N (2024) Fasting as a precursor to high-fat diet enhances mitochondrial resilience in ''Drosophila melanogaster''. Insect Sci [Epub ahead of print]. https://doi.org/10.1111/1744-7917.13355<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38514255 PMID: 38514255 Open Access]<br />
|authors=Hunter-Manseau Florence, Cormier Simon B, Strang Rebekah, Pichaud Nicolas<br />
|year=2024<br />
|journal=Insect Sci<br />
|abstract=Changes in diet type and nutrient availability can impose significant environmental stress on organisms, potentially compromising physiological functions and reproductive success. In nature, dramatic fluctuations in dietary resources are often observed and adjustments to restore cellular homeostasis are crucial to survive this type of stress. In this study, we exposed male ''Drosophila melanogaster'' to two modulated dietary treatments: one without a fasting period before exposure to a high-fat diet and the other with a 24-h fasting period. We then investigated mitochondrial metabolism and molecular responses to these treatments. Exposure to a high-fat diet without a preceding fasting period resulted in disrupted mitochondrial respiration, notably at the level of complex I. On the other hand, a short fasting period before the high-fat diet maintained mitochondrial respiration. Generally, transcript abundance of genes associated with mitophagy, heat-shock proteins, mitochondrial biogenesis, and nutrient sensing pathways increased either slightly or significantly following a fasting period and remained stable when flies were subsequently put on a high-fat diet, whereas a drastic decrease of almost all transcript abundances was observed for all these pathways when flies were exposed directly to a high-fat diet. Moreover, mitochondrial enzymatic activities showed less variation after the fasting period than the treatment without a fasting period. Overall, our study sheds light on the mechanistic protective effects of fasting prior to a high-fat diet and highlights the metabolic flexibility of ''Drosophila'' mitochondria in response to abrupt dietary changes and have implication for adaptation of species to their changing environment.<br />
|keywords=Dietary modulation, Fasting, High‐fat diet, Metabolic flexibility, Mitochondrial metabolism, Stress response<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Drosophila<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Hunter-Manseau_2024_Insect_Sci&diff=246665Hunter-Manseau 2024 Insect Sci2024-03-27T13:37:07Z<p>Plangger Mario: Created page with "{{Publication |title=Hunter-Manseau F, Cormier SB, Strang R, Pichaud N (2024) Fasting as a precursor to high-fat diet enhances mitochondrial resilience in Drosophila melanogas..."</p>
<hr />
<div>{{Publication<br />
|title=Hunter-Manseau F, Cormier SB, Strang R, Pichaud N (2024) Fasting as a precursor to high-fat diet enhances mitochondrial resilience in Drosophila melanogaster. Insect Sci [Epub ahead of print]. https://doi.org/10.1111/1744-7917.13355<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38514255 PMID: 38514255 Open Access]<br />
|authors=Hunter-Manseau F, Cormier SB, Strang R, Pichaud N<br />
|year=2024<br />
|journal=Insect Sci<br />
|abstract=Changes in diet type and nutrient availability can impose significant environmental stress on organisms, potentially compromising physiological functions and reproductive success. In nature, dramatic fluctuations in dietary resources are often observed and adjustments to restore cellular homeostasis are crucial to survive this type of stress. In this study, we exposed male Drosophila melanogaster to two modulated dietary treatments: one without a fasting period before exposure to a high-fat diet and the other with a 24-h fasting period. We then investigated mitochondrial metabolism and molecular responses to these treatments. Exposure to a high-fat diet without a preceding fasting period resulted in disrupted mitochondrial respiration, notably at the level of complex I. On the other hand, a short fasting period before the high-fat diet maintained mitochondrial respiration. Generally, transcript abundance of genes associated with mitophagy, heat-shock proteins, mitochondrial biogenesis, and nutrient sensing pathways increased either slightly or significantly following a fasting period and remained stable when flies were subsequently put on a high-fat diet, whereas a drastic decrease of almost all transcript abundances was observed for all these pathways when flies were exposed directly to a high-fat diet. Moreover, mitochondrial enzymatic activities showed less variation after the fasting period than the treatment without a fasting period. Overall, our study sheds light on the mechanistic protective effects of fasting prior to a high-fat diet and highlights the metabolic flexibility of Drosophila mitochondria in response to abrupt dietary changes and have implication for adaptation of species to their changing environment.<br />
|keywords=Dietary modulation, Fasting, High‐fat diet, Metabolic flexibility, Mitochondrial metabolism, Stress response<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Koumanov_Francoise&diff=246642Koumanov Francoise2024-03-25T11:42:31Z<p>Plangger Mario: </p>
<hr />
<div>{{Person<br />
|lastname=Koumanov<br />
|firstname=Francoise<br />
|title=PhD<br />
|institution=Department for Health, University of Bath<br />
|address=1 West, University of Bath, Claverton Down<br />
|area code=BA2 7AY<br />
|city=Bath<br />
|country=United Kingdom<br />
|mailaddress=F.Koumanov@bath.ac.uk<br />
}}<br />
{{Labelingperson}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Koumanov_Francoise&diff=246641Koumanov Francoise2024-03-25T11:41:25Z<p>Plangger Mario: </p>
<hr />
<div>{{Person<br />
|lastname=Koumanov<br />
|firstname=Francoise<br />
|title=PhD<br />
|institution=Department for Health, University of Bath<br />
|area code=BA2 7AY<br />
|city=Bath<br />
|country=United Kingdom<br />
|mailaddress=F.Koumanov@bath.ac.uk<br />
}}<br />
{{Labelingperson}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Koumanov_Francoise&diff=246640Koumanov Francoise2024-03-25T11:39:06Z<p>Plangger Mario: Created page with "{{Person}}"</p>
<hr />
<div>{{Person}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Shi_2024_Clin_Sci_(Lond)&diff=246530Shi 2024 Clin Sci (Lond)2024-03-15T15:16:05Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Shi L, Yang J, Tao Z, Zheng L, Bui TF, Alonso RL, Yue F, Cheng Z (2024) Loss of FoxO1 activates an alternate mechanism of mitochondrial quality control for healthy adipose browning. Clin Sci (Lond) 138:371-85. https://doi.org/10.1042/cs20230973<br />
|info=[https://www.ncbi.nlm.nih.gov/pubmed/38469619 PMID: 38469619 Open Access]<br />
|authors=Shi Limin, Yang Jinying, Tao Zhipeng, Zheng Louise, Bui Tyler F, Alonso Ramon L, Yue Feng, Cheng Zhiyong<br />
|year=2024<br />
|journal=Clin Sci (Lond)<br />
|abstract=Browning of white adipose tissue is hallmarked by increased mitochondrial density and metabolic improvements. However, it remains largely unknown how mitochondrial turnover and quality control are regulated during adipose browning. In the present study, we found that mice lacking adipocyte FoxO1, a transcription factor that regulates autophagy, adopted an alternate mechanism of mitophagy to maintain mitochondrial turnover and quality control during adipose browning. Post-developmental deletion of adipocyte FoxO1 (adO1KO) suppressed Bnip3 but activated Fundc1/Drp1/OPA1 cascade, concurrent with up-regulation of Atg7 and CTSL. In addition, mitochondrial biogenesis was stimulated via the Pgc1α/Tfam pathway in adO1KO mice. These changes were associated with enhanced mitochondrial homeostasis and metabolic health (e.g., improved glucose tolerance and insulin sensitivity). By contrast, silencing Fundc1 or Pgc1α reversed the changes induced by silencing FoxO1, which impaired mitochondrial quality control and function. Ablation of Atg7 suppressed mitochondrial turnover and function, causing metabolic disorder (e.g., impaired glucose tolerance and insulin sensitivity), regardless of elevated markers of adipose browning. Consistently, suppression of autophagy via CTSL by high-fat diet was associated with a reversal of adO1KO-induced benefits. Our data reveal a unique role of FoxO1 in coordinating mitophagy receptors (Bnip3 and Fundc1) for a fine-tuned mitochondrial turnover and quality control, underscoring autophagic clearance of mitochondria as a prerequisite for healthy browning of adipose tissue.<br />
|keywords=FoxO1, Adipose browning, Metabolism, Mitochondrial quality control, Mitophagy<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Shi_2024_Clin_Sci_(Lond)&diff=246529Shi 2024 Clin Sci (Lond)2024-03-15T15:15:30Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Shi L, Yang J, Tao Z, Zheng L, Bui TF, Alonso RL, Yue F, Cheng Z (2024) Loss of FoxO1 activates an alternate mechanism of mitochondrial quality control for healthy adipose browning. Clin Sci (Lond) 138:371-85. https://doi.org/10.1042/cs20230973<br />
|info=[https://www.ncbi.nlm.nih.gov/pubmed/38469619 PMID: 38469619 Open Access]<br />
|authors=Shi Limin, Yang Jinying, Tao Zhipeng, Zheng Louise, Bui Tyler F, Alonso Ramon L, Yue Feng, Cheng Zhiyong<br />
|year=2024<br />
|journal=Clin Sci (Lond)<br />
|abstract=Browning of white adipose tissue is hallmarked by increased mitochondrial density and metabolic improvements. However, it remains largely unknown how mitochondrial turnover and quality control are regulated during adipose browning. In the present study, we found that mice lacking adipocyte FoxO1, a transcription factor that regulates autophagy, adopted an alternate mechanism of mitophagy to maintain mitochondrial turnover and quality control during adipose browning. Post-developmental deletion of adipocyte FoxO1 (adO1KO) suppressed Bnip3 but activated Fundc1/Drp1/OPA1 cascade, concurrent with up-regulation of Atg7 and CTSL. In addition, mitochondrial biogenesis was stimulated via the Pgc1α/Tfam pathway in adO1KO mice. These changes were associated with enhanced mitochondrial homeostasis and metabolic health (e.g., improved glucose tolerance and insulin sensitivity). By contrast, silencing Fundc1 or Pgc1α reversed the changes induced by silencing FoxO1, which impaired mitochondrial quality control and function. Ablation of Atg7 suppressed mitochondrial turnover and function, causing metabolic disorder (e.g., impaired glucose tolerance and insulin sensitivity), regardless of elevated markers of adipose browning. Consistently, suppression of autophagy via CTSL by high-fat diet was associated with a reversal of adO1KO-induced benefits. Our data reveal a unique role of FoxO1 in coordinating mitophagy receptors (Bnip3 and Fundc1) for a fine-tuned mitochondrial turnover and quality control, underscoring autophagic clearance of mitochondria as a prerequisite for healthy browning of adipose tissue.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Shi_2024_Clin_Sci_(Lond)&diff=246528Shi 2024 Clin Sci (Lond)2024-03-15T13:04:11Z<p>Plangger Mario: Created page with "{{Publication |title=Shi L, Yang J, Tao Z, Zheng L, Bui TF, Alonso RL, Yue F, Cheng Z (2024) Loss of FoxO1 activates an alternate mechanism of mitochondrial quality control fo..."</p>
<hr />
<div>{{Publication<br />
|title=Shi L, Yang J, Tao Z, Zheng L, Bui TF, Alonso RL, Yue F, Cheng Z (2024) Loss of FoxO1 activates an alternate mechanism of mitochondrial quality control for healthy adipose browning. Clin Sci (Lond) 138:371-85. https://doi.org/10.1042/cs20230973<br />
|info=[https://www.ncbi.nlm.nih.gov/pubmed/38469619 PMID: 38469619 Open Access]<br />
|authors=Shi L, Yang J, Tao Z, Zheng L, Bui TF, Alonso RL, Yue F, Cheng Z<br />
|year=2024<br />
|journal=Clin Sci (Lond)<br />
|abstract=Browning of white adipose tissue is hallmarked by increased mitochondrial density and metabolic improvements. However, it remains largely unknown how mitochondrial turnover and quality control are regulated during adipose browning. In the present study, we found that mice lacking adipocyte FoxO1, a transcription factor that regulates autophagy, adopted an alternate mechanism of mitophagy to maintain mitochondrial turnover and quality control during adipose browning. Post-developmental deletion of adipocyte FoxO1 (adO1KO) suppressed Bnip3 but activated Fundc1/Drp1/OPA1 cascade, concurrent with up-regulation of Atg7 and CTSL. In addition, mitochondrial biogenesis was stimulated via the Pgc1α/Tfam pathway in adO1KO mice. These changes were associated with enhanced mitochondrial homeostasis and metabolic health (e.g., improved glucose tolerance and insulin sensitivity). By contrast, silencing Fundc1 or Pgc1α reversed the changes induced by silencing FoxO1, which impaired mitochondrial quality control and function. Ablation of Atg7 suppressed mitochondrial turnover and function, causing metabolic disorder (e.g., impaired glucose tolerance and insulin sensitivity), regardless of elevated markers of adipose browning. Consistently, suppression of autophagy via CTSL by high-fat diet was associated with a reversal of adO1KO-induced benefits. Our data reveal a unique role of FoxO1 in coordinating mitophagy receptors (Bnip3 and Fundc1) for a fine-tuned mitochondrial turnover and quality control, underscoring autophagic clearance of mitochondria as a prerequisite for healthy browning of adipose tissue.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kleinwaechter_2022_RSC_Chem_Biol&diff=246511Kleinwaechter 2022 RSC Chem Biol2024-03-13T15:05:23Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''in vitro'' screening. RSC Chem Biol 3:941-54. https://doi.org/10.1039/d2cb00125j<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/35866160 PMID: 35866160 Open Access]<br />
|authors=Kleinwaechter Isabel, Mohr Bernadette, Joppe Aljoscha, Hellmann Nadja, Bereau Tristan, Osiewacz Heinz D, Schneider Dirk<br />
|year=2022<br />
|journal=RSC Chem Biol<br />
|abstract=Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the ''in silico'' approach were screened ''in vitro'', using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes.<br />
|editor=[[Plangger M]]<br />
|mipnetlab=DE Frankfurt Osiewacz HD<br />
}}<br />
{{Labeling<br />
|area=Respiration, mt-Membrane<br />
|organism=Fungi<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS<br />
|pathways=N, ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kleinwaechter_2022_RSC_Chem_Biol&diff=246510Kleinwaechter 2022 RSC Chem Biol2024-03-13T14:50:50Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''in vitro'' screening. RSC Chem Biol 3:941-54. https://doi.org/10.1039/d2cb00125j<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/35866160 PMID: 35866160 Open Access]<br />
|authors=Kleinwaechter Isabel, Mohr Bernadette, Joppe Aljoscha, Hellmann Nadja, Bereau Tristan, Osiewacz Heinz D, Schneider Dirk<br />
|year=2022<br />
|journal=RSC Chem Biol<br />
|abstract=Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the ''in silico'' approach were screened ''in vitro'', using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes.<br />
|editor=[[Plangger M]]<br />
|mipnetlab=DE Frankfurt Osiewacz HD<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Fungi<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS<br />
|pathways=N, ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kleinwaechter_2022_RSC_Chem_Biol&diff=246509Kleinwaechter 2022 RSC Chem Biol2024-03-13T14:14:13Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''in vitro'' screening. RSC Chem Biol 3:941-54. https://doi.org/10.1039/d2cb00125j<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/35866160 PMID: 35866160 Open Access]<br />
|authors=Kleinwaechter Isabel, Mohr Bernadette, Joppe Aljoscha, Hellmann Nadja, Bereau Tristan, Osiewacz Heinz D, Schneider Dirk<br />
|year=2022<br />
|journal=RSC Chem Biol<br />
|abstract=Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the ''in silico'' approach were screened ''in vitro'', using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes.<br />
|editor=[[Plangger M]]<br />
|mipnetlab=DE Frankfurt Osiewacz HD<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Fungi<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS<br />
|pathways=N<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kleinwaechter_2022_RSC_Chem_Biol&diff=246508Kleinwaechter 2022 RSC Chem Biol2024-03-13T14:04:00Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''in vitro'' screening. RSC Chem Biol 3:941-54. https://doi.org/10.1039/d2cb00125j<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/35866160 PMID: 35866160 Open Access]<br />
|authors=Kleinwaechter Isabel, Mohr Bernadette, Joppe Aljoscha, Hellmann Nadja, Bereau Tristan, Osiewacz Heinz D, Schneider Dirk<br />
|year=2022<br />
|journal=RSC Chem Biol<br />
|abstract=Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the ''in silico'' approach were screened ''in vitro'', using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes.<br />
|editor=[[Plangger M]]<br />
|mipnetlab=DE Frankfurt Osiewacz HD<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS<br />
|pathways=N<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kleinwaechter_2022_RSC_Chem_Biol&diff=246507Kleinwaechter 2022 RSC Chem Biol2024-03-13T13:59:58Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''in vitro'' screening. RSC Chem Biol 3:941-54. https://doi.org/10.1039/d2cb00125j<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/35866160 PMID: 35866160 Open Access]<br />
|authors=Kleinwaechter Isabel, Mohr Bernadette, Joppe Aljoscha, Hellmann Nadja, Bereau Tristan, Osiewacz Heinz D, Schneider Dirk<br />
|year=2022<br />
|journal=RSC Chem Biol<br />
|abstract=Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the ''in silico'' approach were screened ''in vitro'', using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes.<br />
|editor=[[Plangger M]]<br />
|mipnetlab=DE Frankfurt Osiewacz HD<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kleinwaechter_2022_RSC_Chem_Biol&diff=246506Kleinwaechter 2022 RSC Chem Biol2024-03-13T13:59:44Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''in vitro'' screening. RSC Chem Biol 3:941-54. https://doi.org/10.1039/d2cb00125j<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/35866160 PMID: 35866160 Open Access]<br />
|authors=Kleinwaechter Isabel, Mohr Bernadette, Joppe Aljoscha, Hellmann Nadja, Bereau Tristan, Osiewacz Heinz D, Schneider Dirk<br />
|year=2022<br />
|journal=RSC Chem Biol<br />
|abstract=Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the ''in silico'' approach were screened ''in vitro'', using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes.<br />
|editor=[[Plangger M]]<br />
|mipnetlab=DE Frankfurt Osiewacz HD<br />
}}<br />
{{Labeling}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=RSC_Chem_Biol&diff=246505RSC Chem Biol2024-03-13T13:59:20Z<p>Plangger Mario: Created page with "{{Journal |Title=[https://www.rsc.org/journals-books-databases/about-journals/rsc-chemical-biology/ RSC Chemical Biology] }}"</p>
<hr />
<div>{{Journal<br />
|Title=[https://www.rsc.org/journals-books-databases/about-journals/rsc-chemical-biology/ RSC Chemical Biology]<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kleinwaechter_2022_RSC_Chem_Biol&diff=246504Kleinwaechter 2022 RSC Chem Biol2024-03-13T13:58:36Z<p>Plangger Mario: Created page with "{{Publication |title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''i..."</p>
<hr />
<div>{{Publication<br />
|title=Kleinwaechter I, Mohr B, Joppe A, Hellmann N, Bereau T, Osiewacz HD, Schneider D (2022) CLiB - a novel cardiolipin-binder isolated via data-driven and ''in vitro'' screening. RSC Chem Biol 3:941-54. https://doi.org/10.1039/d2cb00125j<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/35866160 PMID: 35866160 Open Access]<br />
|authors=Kleinwaechter Isabel, Mohr Bernadette, Joppe Aljoscha, Hellmann Nadja, Bereau Tristan, Osiewacz Heinz D, Schneider Dirk<br />
|year=2022<br />
|journal=RSC Chem Biol<br />
|abstract=Cardiolipin, the mitochondria marker lipid, is crucially involved in stabilizing the inner mitochondrial membrane and is vital for the activity of mitochondrial proteins and protein complexes. Directly targeting cardiolipin by a chemical-biology approach and thereby altering the cellular concentration of "available" cardiolipin eventually allows to systematically study the dependence of cellular processes on cardiolipin availability. In the present study, physics-based coarse-grained free energy calculations allowed us to identify the physical and chemical properties indicative of cardiolipin selectivity and to apply these to screen a compound database for putative cardiolipin-binders. The membrane binding properties of the 22 most promising molecules identified in the ''in silico'' approach were screened ''in vitro'', using model membrane systems finally resulting in the identification of a single molecule, CLiB (CardioLipin-Binder). CLiB clearly affects respiration of cardiolipin-containing intact bacterial cells as well as of isolated mitochondria. Thus, the structure and function of mitochondrial membranes and membrane proteins might be (indirectly) targeted and controlled by CLiB for basic research and, potentially, also for therapeutic purposes.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Donnelly_2024_EU-METAHEART_MC2_Meeting&diff=246503Donnelly 2024 EU-METAHEART MC2 Meeting2024-03-13T13:53:42Z<p>Plangger Mario: </p>
<hr />
<div>{{Abstract<br />
|title=Donnelly C, Komlódi T, Cecatto C, Cardoso LHD, Kayser B, Place N, Gnaiger E (2024) Functional hypoxia in cardiac mitochondria: effects on oxidative phosphorylation, mitochondrial membrane potential, redox state of coenzyme Q, and calcium uptake. EU-METAHEART MC2 Meeting 2024 Antalya TR.<br />
|info=[[EU-METAHEART]]<br />
|authors=Donnelly Chris, Komlodi Timea, Cecatto Cristiane, Cardoso Luiza HD, Kayser Bengt, Place Nicolas, Gnaiger Erich<br />
|year=2024<br />
|event=EU-METAHEART MC2 Meeting 2024 Antalya TR<br />
|abstract=How changes in respiration under functional hypoxia - i.e., when intracellular O<sub>2</sub> levels limit mitochondrial respiration [1] - are relayed by the electron transfer system to impact mitochondrial adaption and remodeling after hypoxic exposure remains poorly defined. This is largely due to challenges integrating findings under controlled and defined O<sub>2</sub> levels in studies of isolated mitochondria. Performing steady-state respirometry with isolated mouse cardiac mitochondria [2] we found that oxygen limitation of respiration reduced electron flow and oxidative phosphorylation, lowered the mitochondrial membrane potential difference, caused progressive reduction of coenzyme Q, and decreased mitochondrial calcium influx. Our results suggest that by regulating calcium uptake the mitochondrial electron transfer system is a hub for coordinating cellular adaption under functional hypoxia [3].<br />
|editor=[[Plangger M]]<br />
|mipnetlab=AT Innsbruck Oroboros, CH Lausanne Place N, AT Innsbruck Gnaiger E<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|injuries=Hypoxia<br />
|organism=Mouse<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|instruments=Oxygraph-2k<br />
}}<br />
== Affiliations ==<br />
<br />
<br />
== References ==<br />
::::#Donnelly C, Schmitt S, Cecatto C, Cardoso LHD, Komlódi T, Place N, Kayser B, Gnaiger E (2022) The ABC of hypoxia – what is the norm. Bioenerg Commun 2022.12.v2. https://doi.org/10.26124/bec:2022-0012.v2<br />
::::#Harrison DK, Fasching M, Fontana-Ayoub M, Gnaiger E (2015) Cytochrome redox states and respiratory control in mouse and beef heart mitochondria at steady-state levels of hypoxia. J Appl Physiol 119:1210-8. https://doi.org/10.1152/japplphysiol.00146.2015<br />
::::#Donnelly C, Komlódi T, Cecatto C, Cardoso LHD, Compagnion A-C, Matera A, Tavernari D, Campiche O, Paolicelli RC, Zanou N, Kayser B, Gnaiger E, Place N (2024) Functional hypoxia reduces mitochondrial calcium uptake. Redox Biol 71:103037. https://doi.org/10.1016/j.redox.2024.103037</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Donnelly_2024_EU-METAHEART_MC2_Meeting&diff=246502Donnelly 2024 EU-METAHEART MC2 Meeting2024-03-13T13:52:47Z<p>Plangger Mario: </p>
<hr />
<div>{{Abstract<br />
|title=Donnelly C, Komlódi T, Cecatto C, Cardoso LHD, Kayser B, Place N, Gnaiger E (2024) Functional hypoxia in cardiac mitochondria: effects on oxidative phosphorylation, mitochondrial membrane potential, redox state of coenzyme Q, and calcium uptake. EU-METAHEART MC2 Meeting 2024 Antalya TR.<br />
|info=Conference website: tba<br />
|authors=Donnelly Chris, Komlodi Timea, Cecatto Cristiane, Cardoso Luiza HD, Kayser Bengt, Place Nicolas, Gnaiger Erich<br />
|year=2024<br />
|event=EU-METAHEART MC2 Meeting 2024 Antalya TR<br />
|abstract=How changes in respiration under functional hypoxia - i.e., when intracellular O<sub>2</sub> levels limit mitochondrial respiration [1] - are relayed by the electron transfer system to impact mitochondrial adaption and remodeling after hypoxic exposure remains poorly defined. This is largely due to challenges integrating findings under controlled and defined O<sub>2</sub> levels in studies of isolated mitochondria. Performing steady-state respirometry with isolated mouse cardiac mitochondria [2] we found that oxygen limitation of respiration reduced electron flow and oxidative phosphorylation, lowered the mitochondrial membrane potential difference, caused progressive reduction of coenzyme Q, and decreased mitochondrial calcium influx. Our results suggest that by regulating calcium uptake the mitochondrial electron transfer system is a hub for coordinating cellular adaption under functional hypoxia [3].<br />
|editor=[[Plangger M]]<br />
|mipnetlab=AT Innsbruck Oroboros, CH Lausanne Place N, AT Innsbruck Gnaiger E<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|injuries=Hypoxia<br />
|organism=Mouse<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|instruments=Oxygraph-2k<br />
}}<br />
== Affiliations ==<br />
<br />
<br />
== References ==<br />
::::#Donnelly C, Schmitt S, Cecatto C, Cardoso LHD, Komlódi T, Place N, Kayser B, Gnaiger E (2022) The ABC of hypoxia – what is the norm. Bioenerg Commun 2022.12.v2. https://doi.org/10.26124/bec:2022-0012.v2<br />
::::#Harrison DK, Fasching M, Fontana-Ayoub M, Gnaiger E (2015) Cytochrome redox states and respiratory control in mouse and beef heart mitochondria at steady-state levels of hypoxia. J Appl Physiol 119:1210-8. https://doi.org/10.1152/japplphysiol.00146.2015<br />
::::#Donnelly C, Komlódi T, Cecatto C, Cardoso LHD, Compagnion A-C, Matera A, Tavernari D, Campiche O, Paolicelli RC, Zanou N, Kayser B, Gnaiger E, Place N (2024) Functional hypoxia reduces mitochondrial calcium uptake. Redox Biol 71:103037. https://doi.org/10.1016/j.redox.2024.103037</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Glombik_2023_Int_J_Mol_Sci&diff=246501Glombik 2023 Int J Mol Sci2024-03-13T13:49:40Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Glombik K, Kukla-Bartoszek M, Curzytek K, Detka J, Basta-Kaim A, Budziszewska B (2023) The effects of prenatal dexamethasone exposure on brain metabolic homeostasis in adulthood: implications for depression. Int J Mol Sci 24:1156. https://doi.org/10.3390/ijms24021156<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36674678 PMID: 36674678 Open Access]<br />
|authors=Glombik Katarzyna, Kukla-Bartoszek Magdalena, Curzytek Katarzyna, Detka Jan, Basta-Kaim Agnieszka, Budziszewska Boguslawa<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=Since depression produces a long-term negative impact on quality of life, understanding the pathophysiological changes implicated in this disorder is urgent. There is growing evidence that demonstrates a key role for dysfunctional energy metabolism in driving the onset of depression; thus, bioenergetic alterations should be extensively studied. Brain metabolism is known to be a glucocorticoid-sensitive process, but the long-lasting consequences in adulthood following high levels of glucocorticoids at the early stages of life are unclear. We examined a possible association between brain energetic changes induced by synthetic glucocorticoid-dexamethasone treatment in the prenatal period and depressive-like behavior. The results show a reduction in the oxidative phosphorylation process, Krebs cycle impairment, and a weakening of the connection between the Krebs cycle and glycolysis in the frontal cortex of animals receiving dexamethasone, which leads to ATP reduction. These changes appear to be mainly due to decreased expression of pyruvate dehydrogenase, impairment of lactate transport to neurons, and pyruvate to the mitochondria. Acute stress in adulthood only slightly modified the observed alterations in the frontal cortex, while in the case of the hippocampus, prenatal exposure to dexamethasone made this structure more sensitive to future adverse factors.<br />
|keywords=Animal model, Bioenergetics, Brain, Depression, Dexamethasone<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration, Developmental biology<br />
|diseases=Other<br />
|organism=Rat<br />
|tissues=Nervous system<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS, ET<br />
|pathways=N, S, NS, ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Glombik_2023_Int_J_Mol_Sci&diff=246498Glombik 2023 Int J Mol Sci2024-03-13T13:39:42Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Glombik K, Kukla-Bartoszek M, Curzytek K, Detka J, Basta-Kaim A, Budziszewska B (2023) The effects of prenatal dexamethasone exposure on brain metabolic homeostasis in adulthood: implications for depression. Int J Mol Sci 24:1156. https://doi.org/10.3390/ijms24021156<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36674678 PMID: 36674678 Open Access]<br />
|authors=Glombik Katarzyna, Kukla-Bartoszek Magdalena, Curzytek Katarzyna, Detka Jan, Basta-Kaim Agnieszka, Budziszewska Boguslawa<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=Since depression produces a long-term negative impact on quality of life, understanding the pathophysiological changes implicated in this disorder is urgent. There is growing evidence that demonstrates a key role for dysfunctional energy metabolism in driving the onset of depression; thus, bioenergetic alterations should be extensively studied. Brain metabolism is known to be a glucocorticoid-sensitive process, but the long-lasting consequences in adulthood following high levels of glucocorticoids at the early stages of life are unclear. We examined a possible association between brain energetic changes induced by synthetic glucocorticoid-dexamethasone treatment in the prenatal period and depressive-like behavior. The results show a reduction in the oxidative phosphorylation process, Krebs cycle impairment, and a weakening of the connection between the Krebs cycle and glycolysis in the frontal cortex of animals receiving dexamethasone, which leads to ATP reduction. These changes appear to be mainly due to decreased expression of pyruvate dehydrogenase, impairment of lactate transport to neurons, and pyruvate to the mitochondria. Acute stress in adulthood only slightly modified the observed alterations in the frontal cortex, while in the case of the hippocampus, prenatal exposure to dexamethasone made this structure more sensitive to future adverse factors.<br />
|keywords=Animal model, Bioenergetics, Brain, Depression, Dexamethasone<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Glombik_2023_Int_J_Mol_Sci&diff=246497Glombik 2023 Int J Mol Sci2024-03-13T13:38:23Z<p>Plangger Mario: Created page with "{{Publication |title=Glombik K, Kukla-Bartoszek M, Curzytek K, Detka J, Basta-Kaim A, Budziszewska B (2023) The effects of prenatal dexamethasone exposure on brain metabolic h..."</p>
<hr />
<div>{{Publication<br />
|title=Glombik K, Kukla-Bartoszek M, Curzytek K, Detka J, Basta-Kaim A, Budziszewska B (2023) The effects of prenatal dexamethasone exposure on brain metabolic homeostasis in adulthood: implications for depression. Int J Mol Sci 24:1156. https://doi.org/10.3390/ijms24021156<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36674678 PMID: 36674678 Open Access]<br />
|authors=Glombik K, Kukla-Bartoszek M, Curzytek K, Detka J, Basta-Kaim A, Budziszewska B<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=Since depression produces a long-term negative impact on quality of life, understanding the pathophysiological changes implicated in this disorder is urgent. There is growing evidence that demonstrates a key role for dysfunctional energy metabolism in driving the onset of depression; thus, bioenergetic alterations should be extensively studied. Brain metabolism is known to be a glucocorticoid-sensitive process, but the long-lasting consequences in adulthood following high levels of glucocorticoids at the early stages of life are unclear. We examined a possible association between brain energetic changes induced by synthetic glucocorticoid-dexamethasone treatment in the prenatal period and depressive-like behavior. The results show a reduction in the oxidative phosphorylation process, Krebs cycle impairment, and a weakening of the connection between the Krebs cycle and glycolysis in the frontal cortex of animals receiving dexamethasone, which leads to ATP reduction. These changes appear to be mainly due to decreased expression of pyruvate dehydrogenase, impairment of lactate transport to neurons, and pyruvate to the mitochondria. Acute stress in adulthood only slightly modified the observed alterations in the frontal cortex, while in the case of the hippocampus, prenatal exposure to dexamethasone made this structure more sensitive to future adverse factors.<br />
|keywords=Animal model, Bioenergetics, Brain, Depression, Dexamethasone<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Verma_2023_Int_J_Mol_Sci&diff=246496Verma 2023 Int J Mol Sci2024-03-13T13:28:45Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Verma A, Azhar G, Zhang X, Patyal P, Kc G, Sharma S, Che Y, Wei JY (2023) ''P. gingivalis''-LPS induces mitochondrial dysfunction mediated by neuroinflammation through oxidative stress. Int J Mol Sci 24:950. https://doi.org/10.3390/ijms24020950<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36674463 PMID: 36674463 Open Access]<br />
|authors=Verma Ambika, Azhar Gohar, Zhang Xiaomin, Patyal Pankaj, Kc Grishma, Sharma Shakshi, Che Yingni, Wei Jeanne Y<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=''Porphyromonas gingivalis'' (''P. gingivalis''), a key pathogen in periodontitis, is associated with neuroinflammation. Periodontal disease increases with age; 70.1% of adults 65 years and older have periodontal problems. However, the ''P. gingivalis''- lipopolysaccharide (LPS)induced mitochondrial dysfunction in neurodegenerative diseases remains elusive. In this study, we investigated the possible role of ''P. gingivalis''-LPS in mitochondrial dysfunction during neurodegeneration. We found that ''P. gingivalis''-LPS treatment activated toll-like receptor (TLR) 4 signaling and upregulated the expression of Alzheimer's disease-related dementia and neuroinflammatory markers. Furthermore, the LPS treatment significantly exacerbated the production of reactive oxygen species and reduced the mitochondrial membrane potential. Our study highlighted the pivotal role of ''P. gingivalis''-LPS in the repression of serum response factor (SRF) and its co-factor p49/STRAP that regulate the actin cytoskeleton. The LPS treatment repressed the genes involved in mitochondrial function and biogenesis. ''P. gingivalis''-LPS negatively altered oxidative phosphorylation and glycolysis and reduced total adenosine triphosphate (ATP) production. Additionally, it specifically altered the mitochondrial functions in complexes I, II, and IV of the mitochondrial electron transport chain. Thus, it is conceivable that ''P. gingivalis''-LPS causes mitochondrial dysfunction through oxidative stress and inflammatory events in neurodegenerative diseases.<br />
|keywords=P. gingivalis-LPS, Mitochondrial dysfunction, Neuroinflammation, Oxidative stress<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|diseases=Neurodegenerative<br />
|organism=Human<br />
|tissues=Endothelial;epithelial;mesothelial cell<br />
|preparations=Permeabilized cells, Intact cells<br />
|couplingstates=LEAK, ROUTINE, OXPHOS, ET<br />
|pathways=N, S, CIV, ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Verma_2023_Int_J_Mol_Sci&diff=246495Verma 2023 Int J Mol Sci2024-03-13T13:19:28Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Verma A, Azhar G, Zhang X, Patyal P, Kc G, Sharma S, Che Y, Wei JY (2023) ''P. gingivalis''-LPS induces mitochondrial dysfunction mediated by neuroinflammation through oxidative stress. Int J Mol Sci 24:950. https://doi.org/10.3390/ijms24020950<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36674463 PMID: 36674463 Open Access]<br />
|authors=Verma Ambika, Azhar Gohar, Zhang Xiaomin, Patyal Pankaj, Kc Grishma, Sharma Shakshi, Che Yingni, Wei Jeanne Y<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=''Porphyromonas gingivalis'' (''P. gingivalis''), a key pathogen in periodontitis, is associated with neuroinflammation. Periodontal disease increases with age; 70.1% of adults 65 years and older have periodontal problems. However, the ''P. gingivalis''- lipopolysaccharide (LPS)induced mitochondrial dysfunction in neurodegenerative diseases remains elusive. In this study, we investigated the possible role of ''P. gingivalis''-LPS in mitochondrial dysfunction during neurodegeneration. We found that ''P. gingivalis''-LPS treatment activated toll-like receptor (TLR) 4 signaling and upregulated the expression of Alzheimer's disease-related dementia and neuroinflammatory markers. Furthermore, the LPS treatment significantly exacerbated the production of reactive oxygen species and reduced the mitochondrial membrane potential. Our study highlighted the pivotal role of ''P. gingivalis''-LPS in the repression of serum response factor (SRF) and its co-factor p49/STRAP that regulate the actin cytoskeleton. The LPS treatment repressed the genes involved in mitochondrial function and biogenesis. ''P. gingivalis''-LPS negatively altered oxidative phosphorylation and glycolysis and reduced total adenosine triphosphate (ATP) production. Additionally, it specifically altered the mitochondrial functions in complexes I, II, and IV of the mitochondrial electron transport chain. Thus, it is conceivable that ''P. gingivalis''-LPS causes mitochondrial dysfunction through oxidative stress and inflammatory events in neurodegenerative diseases.<br />
|keywords=P. gingivalis-LPS, Mitochondrial dysfunction, Neuroinflammation, Oxidative stress<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Verma_2023_Int_J_Mol_Sci&diff=246494Verma 2023 Int J Mol Sci2024-03-13T13:15:46Z<p>Plangger Mario: Created page with "{{Publication |title=Verma A, Azhar G, Zhang X, Patyal P, Kc G, Sharma S, Che Y, Wei JY (2023) ''P. gingivalis''-LPS induces mitochondrial dysfunction mediated by neuroinflamm..."</p>
<hr />
<div>{{Publication<br />
|title=Verma A, Azhar G, Zhang X, Patyal P, Kc G, Sharma S, Che Y, Wei JY (2023) ''P. gingivalis''-LPS induces mitochondrial dysfunction mediated by neuroinflammation through oxidative stress. Int J Mol Sci 24:950. https://doi.org/10.3390/ijms24020950<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36674463 PMID: 36674463 Open Access]<br />
|authors=Verma A, Azhar G, Zhang X, Patyal P, Kc G, Sharma S, Che Y, Wei JY<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=Porphyromonas gingivalis (P. gingivalis), a key pathogen in periodontitis, is associated with neuroinflammation. Periodontal disease increases with age; 70.1% of adults 65 years and older have periodontal problems. However, the P. gingivalis- lipopolysaccharide (LPS)induced mitochondrial dysfunction in neurodegenerative diseases remains elusive. In this study, we investigated the possible role of P. gingivalis-LPS in mitochondrial dysfunction during neurodegeneration. We found that P. gingivalis-LPS treatment activated toll-like receptor (TLR) 4 signaling and upregulated the expression of Alzheimer's disease-related dementia and neuroinflammatory markers. Furthermore, the LPS treatment significantly exacerbated the production of reactive oxygen species and reduced the mitochondrial membrane potential. Our study highlighted the pivotal role of P. gingivalis-LPS in the repression of serum response factor (SRF) and its co-factor p49/STRAP that regulate the actin cytoskeleton. The LPS treatment repressed the genes involved in mitochondrial function and biogenesis. P. gingivalis-LPS negatively altered oxidative phosphorylation and glycolysis and reduced total adenosine triphosphate (ATP) production. Additionally, it specifically altered the mitochondrial functions in complexes I, II, and IV of the mitochondrial electron transport chain. Thus, it is conceivable that P. gingivalis-LPS causes mitochondrial dysfunction through oxidative stress and inflammatory events in neurodegenerative diseases.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Bassot_2023_Cell_Rep&diff=246493Bassot 2023 Cell Rep2024-03-13T13:09:55Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Bassot A, Chen J, Takahashi-Yamashiro K, Yap MC, Gibhardt CS, Le GNT, Hario S, Nasu Y, Moore J, Gutiérrez T, Mina L, Mast H, Moses A, Bhat R, Ballanyi K, Lemieux H, Sitia R, Zito E, Bogeski I, Campbell RE, Simmen T (2023) The endoplasmic reticulum kinase PERK interacts with the oxidoreductase ERO1 to metabolically adapt mitochondria. Cell Rep 42:111899. https://doi.org/10.1016/j.celrep.2022.111899<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36586409 PMID: 36586409 Open Access]<br />
|authors=Bassot Arthur, Chen Junsheng, Takahashi-Yamashiro Kei, Yap Megan C, Gibhardt Christine Silvia, Le Giang NT, Hario Saaya, Nasu Yusuke, Moore Jack, Gutierrez Tomas, Mina Lucas, Mast Heather, Moses Audric, Bhat Rakesh, Ballanyi Klaus, Lemieux Helene, Sitia Roberto, Zito Ester, Bogeski Ivan, Campbell Robert E, Simmen Thomas<br />
|year=2023<br />
|journal=Cell Rep<br />
|abstract=Endoplasmic reticulum (ER) homeostasis requires molecular regulators that tailor mitochondrial bioenergetics to the needs of protein folding. For instance, calnexin maintains mitochondria metabolism and mitochondria-ER contacts (MERCs) through reactive oxygen species (ROS) from NADPH oxidase 4 (NOX4). However, induction of ER stress requires a quick molecular rewiring of mitochondria to adapt to new energy needs. This machinery is not characterized. We now show that the oxidoreductase ERO1⍺ covalently interacts with protein kinase RNA-like ER kinase (PERK) upon treatment with tunicamycin. The PERK-ERO1⍺ interaction requires the C-terminal active site of ERO1⍺ and cysteine 216 of PERK. Moreover, we show that the PERK-ERO1⍺ complex promotes oxidization of MERC proteins and controls mitochondrial dynamics. Using proteinaceous probes, we determined that these functions improve ER-mitochondria Ca<sup>2+</sup> flux to maintain bioenergetics in both organelles, while limiting oxidative stress. Therefore, the PERK-ERO1⍺ complex is a key molecular machinery that allows quick metabolic adaptation to ER stress.<br />
|keywords=CP: Metabolism, CP: Molecular biology, ER, ER stress, ERO1, MAMs, MERCs, PERK, Bioenergetics, Endoplasmic reticulum, Mitochondria, Mitochondria-associated membranes, Mitochondria-endoplasmic reticulum contacts, Oxidoreductase<br />
|editor=[[Plangger M]]<br />
|mipnetlab=CA Edmonton Lemieux H<br />
}}<br />
{{Labeling<br />
|area=Respiration, Genetic knockout;overexpression<br />
|organism=Human, Mouse<br />
|tissues=HEK, Fibroblast<br />
|preparations=Intact cells<br />
|couplingstates=LEAK, ROUTINE, ET<br />
|pathways=ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Bassot_2023_Cell_Rep&diff=246492Bassot 2023 Cell Rep2024-03-13T12:53:53Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Bassot A, Chen J, Takahashi-Yamashiro K, Yap MC, Gibhardt CS, Le GNT, Hario S, Nasu Y, Moore J, Gutiérrez T, Mina L, Mast H, Moses A, Bhat R, Ballanyi K, Lemieux H, Sitia R, Zito E, Bogeski I, Campbell RE, Simmen T (2023) The endoplasmic reticulum kinase PERK interacts with the oxidoreductase ERO1 to metabolically adapt mitochondria. Cell Rep 42:111899. https://doi.org/10.1016/j.celrep.2022.111899<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36586409 PMID: 36586409 Open Access]<br />
|authors=Bassot Arthur, Chen Junsheng, Takahashi-Yamashiro Kei, Yap Megan C, Gibhardt Christine Silvia, Le Giang NT, Hario Saaya, Nasu Yusuke, Moore Jack, Gutierrez Tomas, Mina Lucas, Mast Heather, Moses Audric, Bhat Rakesh, Ballanyi Klaus, Lemieux Helene, Sitia Roberto, Zito Ester, Bogeski Ivan, Campbell Robert E, Simmen Thomas<br />
|year=2023<br />
|journal=Cell Rep<br />
|abstract=Endoplasmic reticulum (ER) homeostasis requires molecular regulators that tailor mitochondrial bioenergetics to the needs of protein folding. For instance, calnexin maintains mitochondria metabolism and mitochondria-ER contacts (MERCs) through reactive oxygen species (ROS) from NADPH oxidase 4 (NOX4). However, induction of ER stress requires a quick molecular rewiring of mitochondria to adapt to new energy needs. This machinery is not characterized. We now show that the oxidoreductase ERO1⍺ covalently interacts with protein kinase RNA-like ER kinase (PERK) upon treatment with tunicamycin. The PERK-ERO1⍺ interaction requires the C-terminal active site of ERO1⍺ and cysteine 216 of PERK. Moreover, we show that the PERK-ERO1⍺ complex promotes oxidization of MERC proteins and controls mitochondrial dynamics. Using proteinaceous probes, we determined that these functions improve ER-mitochondria Ca<sup>2+</sup> flux to maintain bioenergetics in both organelles, while limiting oxidative stress. Therefore, the PERK-ERO1⍺ complex is a key molecular machinery that allows quick metabolic adaptation to ER stress.<br />
|keywords=CP: Metabolism, CP: Molecular biology, ER, ER stress, ERO1, MAMs, MERCs, PERK, Bioenergetics, Endoplasmic reticulum, Mitochondria, Mitochondria-associated membranes, Mitochondria-endoplasmic reticulum contacts, Oxidoreductase<br />
|editor=[[Plangger M]]<br />
|mipnetlab=CA Edmonton Lemieux H<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Human, Mouse<br />
|tissues=HEK, Fibroblast<br />
|preparations=Intact cells<br />
|couplingstates=LEAK, ROUTINE, ET<br />
|pathways=ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Bassot_2023_Cell_Rep&diff=246491Bassot 2023 Cell Rep2024-03-13T12:45:04Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Bassot A, Chen J, Takahashi-Yamashiro K, Yap MC, Gibhardt CS, Le GNT, Hario S, Nasu Y, Moore J, Gutiérrez T, Mina L, Mast H, Moses A, Bhat R, Ballanyi K, Lemieux H, Sitia R, Zito E, Bogeski I, Campbell RE, Simmen T (2023) The endoplasmic reticulum kinase PERK interacts with the oxidoreductase ERO1 to metabolically adapt mitochondria. Cell Rep 42:111899. https://doi.org/10.1016/j.celrep.2022.111899<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36586409 PMID: 36586409 Open Access]<br />
|authors=Bassot Arthur, Chen Junsheng, Takahashi-Yamashiro Kei, Yap Megan C, Gibhardt Christine Silvia, Le Giang NT, Hario Saaya, Nasu Yusuke, Moore Jack, Gutierrez Tomas, Mina Lucas, Mast Heather, Moses Audric, Bhat Rakesh, Ballanyi Klaus, Lemieux Helene, Sitia Roberto, Zito Ester, Bogeski Ivan, Campbell Robert E, Simmen Thomas<br />
|year=2023<br />
|journal=Cell Rep<br />
|abstract=Endoplasmic reticulum (ER) homeostasis requires molecular regulators that tailor mitochondrial bioenergetics to the needs of protein folding. For instance, calnexin maintains mitochondria metabolism and mitochondria-ER contacts (MERCs) through reactive oxygen species (ROS) from NADPH oxidase 4 (NOX4). However, induction of ER stress requires a quick molecular rewiring of mitochondria to adapt to new energy needs. This machinery is not characterized. We now show that the oxidoreductase ERO1⍺ covalently interacts with protein kinase RNA-like ER kinase (PERK) upon treatment with tunicamycin. The PERK-ERO1⍺ interaction requires the C-terminal active site of ERO1⍺ and cysteine 216 of PERK. Moreover, we show that the PERK-ERO1⍺ complex promotes oxidization of MERC proteins and controls mitochondrial dynamics. Using proteinaceous probes, we determined that these functions improve ER-mitochondria Ca<sup>2+</sup> flux to maintain bioenergetics in both organelles, while limiting oxidative stress. Therefore, the PERK-ERO1⍺ complex is a key molecular machinery that allows quick metabolic adaptation to ER stress.<br />
|keywords=CP: Metabolism, CP: Molecular biology, ER, ER stress, ERO1, MAMs, MERCs, PERK, Bioenergetics, Endoplasmic reticulum, Mitochondria, Mitochondria-associated membranes, Mitochondria-endoplasmic reticulum contacts, Oxidoreductase<br />
|editor=[[Plangger M]]<br />
|mipnetlab=CA Edmonton Lemieux H<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Bassot_2023_Cell_Rep&diff=246490Bassot 2023 Cell Rep2024-03-13T12:42:06Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Bassot A, Chen J, Takahashi-Yamashiro K, Yap MC, Gibhardt CS, Le GNT, Hario S, Nasu Y, Moore J, Gutiérrez T, Mina L, Mast H, Moses A, Bhat R, Ballanyi K, Lemieux H, Sitia R, Zito E, Bogeski I, Campbell RE, Simmen T (2023) The endoplasmic reticulum kinase PERK interacts with the oxidoreductase ERO1 to metabolically adapt mitochondria. Cell Rep 42:111899. https://doi.org/10.1016/j.celrep.2022.111899<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36586409 PMID: 36586409 Open Access]<br />
|authors=Bassot Arthur, Chen Junsheng, Takahashi-Yamashiro Kei, Yap Megan C, Gibhardt Christine Silvia, Le Giang NT, Hario Saaya, Nasu Yusuke, Moore Jack, Gutierrez Tomas, Mina Lucas, Mast Heather, Moses Audric, Bhat Rakesh, Ballanyi Klaus, Lemieux Helene, Sitia Roberto, Zito Ester, Bogeski Ivan, Campbell Robert E, Simmen Thomas<br />
|year=2023<br />
|journal=Cell Rep<br />
|abstract=Endoplasmic reticulum (ER) homeostasis requires molecular regulators that tailor mitochondrial bioenergetics to the needs of protein folding. For instance, calnexin maintains mitochondria metabolism and mitochondria-ER contacts (MERCs) through reactive oxygen species (ROS) from NADPH oxidase 4 (NOX4). However, induction of ER stress requires a quick molecular rewiring of mitochondria to adapt to new energy needs. This machinery is not characterized. We now show that the oxidoreductase ERO1⍺ covalently interacts with protein kinase RNA-like ER kinase (PERK) upon treatment with tunicamycin. The PERK-ERO1⍺ interaction requires the C-terminal active site of ERO1⍺ and cysteine 216 of PERK. Moreover, we show that the PERK-ERO1⍺ complex promotes oxidization of MERC proteins and controls mitochondrial dynamics. Using proteinaceous probes, we determined that these functions improve ER-mitochondria Ca<sup>2+</sup> flux to maintain bioenergetics in both organelles, while limiting oxidative stress. Therefore, the PERK-ERO1⍺ complex is a key molecular machinery that allows quick metabolic adaptation to ER stress.<br />
|keywords=CP: Metabolism, CP: Molecular biology, ER, ER stress, ERO1, MAMs, MERCs, PERK, Bioenergetics, Endoplasmic reticulum, Mitochondria, Mitochondria-associated membranes, Mitochondria-endoplasmic reticulum contacts, Oxidoreductase<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Bassot_2023_Cell_Rep&diff=246489Bassot 2023 Cell Rep2024-03-13T12:37:05Z<p>Plangger Mario: Created page with "{{Publication |title=Bassot A, Chen J, Takahashi-Yamashiro K, Yap MC, Gibhardt CS, Le GNT, Hario S, Nasu Y, Moore J, Gutiérrez T, Mina L, Mast H, Moses A, Bhat R, Ballanyi K,..."</p>
<hr />
<div>{{Publication<br />
|title=Bassot A, Chen J, Takahashi-Yamashiro K, Yap MC, Gibhardt CS, Le GNT, Hario S, Nasu Y, Moore J, Gutiérrez T, Mina L, Mast H, Moses A, Bhat R, Ballanyi K, Lemieux H, Sitia R, Zito E, Bogeski I, Campbell RE, Simmen T (2023) The endoplasmic reticulum kinase PERK interacts with the oxidoreductase ERO1 to metabolically adapt mitochondria. Cell Rep 42:111899. https://doi.org/10.1016/j.celrep.2022.111899<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36586409 PMID: 36586409 Open Access]<br />
|authors=Bassot A, Chen J, Takahashi-Yamashiro K, Yap MC, Gibhardt CS, Le GNT, Hario S, Nasu Y, Moore J, Gutiérrez T, Mina L, Mast H, Moses A, Bhat R, Ballanyi K, Lemieux H, Sitia R, Zito E, Bogeski I, Campbell RE, Simmen T<br />
|year=2023<br />
|journal=Cell Rep<br />
|abstract=Endoplasmic reticulum (ER) homeostasis requires molecular regulators that tailor mitochondrial bioenergetics to the needs of protein folding. For instance, calnexin maintains mitochondria metabolism and mitochondria-ER contacts (MERCs) through reactive oxygen species (ROS) from NADPH oxidase 4 (NOX4). However, induction of ER stress requires a quick molecular rewiring of mitochondria to adapt to new energy needs. This machinery is not characterized. We now show that the oxidoreductase ERO1⍺ covalently interacts with protein kinase RNA-like ER kinase (PERK) upon treatment with tunicamycin. The PERK-ERO1⍺ interaction requires the C-terminal active site of ERO1⍺ and cysteine 216 of PERK. Moreover, we show that the PERK-ERO1⍺ complex promotes oxidization of MERC proteins and controls mitochondrial dynamics. Using proteinaceous probes, we determined that these functions improve ER-mitochondria Ca2+ flux to maintain bioenergetics in both organelles, while limiting oxidative stress. Therefore, the PERK-ERO1⍺ complex is a key molecular machinery that allows quick metabolic adaptation to ER stress.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Dabrowska_2023_Int_J_Mol_Sci&diff=246488Dabrowska 2023 Int J Mol Sci2024-03-13T12:34:33Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Dabrowska A, Zajac M, Bednarczyk P, Lukasiak A (2023) Effect of quercetin on mitoBK<sub>Ca</sub> channel and mitochondrial function in human bronchial epithelial cells exposed to particulate matter. Int J Mol Sci 24:638. https://doi.org/10.3390/ijms24010638<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36614079 PMID: 36614079 Open Access]<br />
|authors=Dabrowska Adrianna, Zajac Miroslaw, Bednarczyk Piotr, Lukasiak Agnieszka<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=Particulate matter (PM) exposure increases reactive oxygen species (ROS) levels. It can lead to inflammatory responses and damage of the mitochondria thus inducing cell death. Recently, it has been shown that potassium channels (mitoK) located in the inner mitochondrial membrane are involved in cytoprotection, and one of the mechanisms involves ROS. To verify the cytoprotective role of mitoBK<sub>Ca</sub>, we performed a series of experiments using a patch-clamp, transepithelial electrical resistance assessment (TEER), mitochondrial respiration measurements, fluorescence methods for the ROS level and mitochondrial membrane potential assessment, and cell viability measurements. In the human bronchial epithelial cell model (16HBE14σ), PM < 4 μm in diameter (SRM-PM4.0) was used. We observed that PM decreased TEER of HBE cell monolayers. The effect was partially abolished by quercetin, a mitoBK<sub>Ca</sub> opener. Consequently, quercetin decreased the mitochondrial membrane potential and increased mitochondrial respiration. The reduction of PM-induced ROS level occurs both on cellular and mitochondrial level. Additionally, quercetin restores HBE cell viability after PM administration. The incubation of cells with PM substantially reduced the mitochondrial function. Isorhamnetin had no effect on TEER, the mitoBK<sub>Ca</sub> activity, respiratory rate, or mitochondrial membrane potential. Obtained results indicate that PM has an adverse effect on HBE cells at the cellular and mitochondrial level. Quercetin is able to limit the deleterious effect of PM on barrier function of airway epithelial cells. We show that the effect in HBE cells involves mitoBK<sub>Ca</sub> channel-activation. However, quercetin’s mechanism of action is not exclusively determined by modulation of the channel activity.<br />
|keywords=Epithelium, mitoBKCa channel, Mitochondria, Particulate matter, Quercetin<br />
|editor=[[Plangger M]]<br />
|mipnetlab=PL Warsaw Bednarczyk P<br />
}}<br />
{{Labeling<br />
|area=Respiration, mt-Membrane, Pharmacology;toxicology<br />
|injuries=Oxidative stress;RONS<br />
|organism=Human<br />
|tissues=Lung;gill, Endothelial;epithelial;mesothelial cell<br />
|preparations=Permeabilized cells, Intact cells<br />
|topics=Ion;substrate transport, mt-Membrane potential<br />
|couplingstates=LEAK, ROUTINE, OXPHOS, ET<br />
|pathways=S, ROX<br />
|instruments=Oxygraph-2k, O2k-Fluorometer<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Dabrowska_2023_Int_J_Mol_Sci&diff=246487Dabrowska 2023 Int J Mol Sci2024-03-13T12:23:13Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Dabrowska A, Zajac M, Bednarczyk P, Lukasiak A (2023) Effect of Quercetin on mito<sub>BKCa</sub> channel and mitochondrial function in human bronchial epithelial cells exposed to particulate matter. Int J Mol Sci 24:638. https://doi.org/10.3390/ijms24010638<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36614079 PMID: 36614079 Open Access]<br />
|authors=Dabrowska Adrianna, Zajac Miroslaw, Bednarczyk Piotr, Lukasiak Agnieszka<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=Particulate matter (PM) exposure increases reactive oxygen species (ROS) levels. It can lead to inflammatory responses and damage of the mitochondria thus inducing cell death. Recently, it has been shown that potassium channels (mitoK) located in the inner mitochondrial membrane are involved in cytoprotection, and one of the mechanisms involves ROS. To verify the cytoprotective role of mito<sub>BKCa</sub>, we performed a series of experiments using a patch-clamp, transepithelial electrical resistance assessment (TEER), mitochondrial respiration measurements, fluorescence methods for the ROS level and mitochondrial membrane potential assessment, and cell viability measurements. In the human bronchial epithelial cell model (16HBE14σ), PM < 4 μm in diameter (SRM-PM4.0) was used. We observed that PM decreased TEER of HBE cell monolayers. The effect was partially abolished by quercetin, a mito<sub>BKCa</sub> opener. Consequently, quercetin decreased the mitochondrial membrane potential and increased mitochondrial respiration. The reduction of PM-induced ROS level occurs both on cellular and mitochondrial level. Additionally, quercetin restores HBE cell viability after PM administration. The incubation of cells with PM substantially reduced the mitochondrial function. Isorhamnetin had no effect on TEER, the mito<sub>BKCa</sub> activity, respiratory rate, or mitochondrial membrane potential. Obtained results indicate that PM has an adverse effect on HBE cells at the cellular and mitochondrial level. Quercetin is able to limit the deleterious effect of PM on barrier function of airway epithelial cells. We show that the effect in HBE cells involves mitomito<sub>BKCa</sub> channel-activation. However, quercetin’s mechanism of action is not exclusively determined by modulation of the channel activity.<br />
|keywords=Epithelium, mitoBKCa channel, Mitochondria, Particulate matter, Quercetin<br />
|editor=[[Plangger M]]<br />
|mipnetlab=PL Warsaw Bednarczyk P<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Dabrowska_2023_Int_J_Mol_Sci&diff=246486Dabrowska 2023 Int J Mol Sci2024-03-13T12:22:08Z<p>Plangger Mario: Created page with "{{Publication |title=Dabrowska A, Zajac M, Bednarczyk P, Lukasiak A (2023) Effect of Quercetin on mito<sub>BKCa</sub> channel and mitochondrial function in human bronchial epi..."</p>
<hr />
<div>{{Publication<br />
|title=Dabrowska A, Zajac M, Bednarczyk P, Lukasiak A (2023) Effect of Quercetin on mito<sub>BKCa</sub> channel and mitochondrial function in human bronchial epithelial cells exposed to particulate matter. Int J Mol Sci 24:638. https://doi.org/10.3390/ijms24010638<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/36614079 PMID: 36614079 Open Access]<br />
|authors=Dabrowska Adrianna, Zajac Miroslaw, Bednarczyk Piotr, Lukasiak Agnieszka<br />
|year=2023<br />
|journal=Int J Mol Sci<br />
|abstract=Particulate matter (PM) exposure increases reactive oxygen species (ROS) levels. It can lead to inflammatory responses and damage of the mitochondria thus inducing cell death. Recently, it has been shown that potassium channels (mitoK) located in the inner mitochondrial membrane are involved in cytoprotection, and one of the mechanisms involves ROS. To verify the cytoprotective role of mitoBKCa, we performed a series of experiments using a patch-clamp, transepithelial electrical resistance assessment (TEER), mitochondrial respiration measurements, fluorescence methods for the ROS level and mitochondrial membrane potential assessment, and cell viability measurements. In the human bronchial epithelial cell model (16HBE14σ), PM < 4 μm in diameter (SRM-PM4.0) was used. We observed that PM decreased TEER of HBE cell monolayers. The effect was partially abolished by quercetin, a mitoBKCa opener. Consequently, quercetin decreased the mitochondrial membrane potential and increased mitochondrial respiration. The reduction of PM-induced ROS level occurs both on cellular and mitochondrial level. Additionally, quercetin restores HBE cell viability after PM administration. The incubation of cells with PM substantially reduced the mitochondrial function. Isorhamnetin had no effect on TEER, the mitoBKCa activity, respiratory rate, or mitochondrial membrane potential. Obtained results indicate that PM has an adverse effect on HBE cells at the cellular and mitochondrial level. Quercetin is able to limit the deleterious effect of PM on barrier function of airway epithelial cells. We show that the effect in HBE cells involves mitoBKCa channel-activation. However, quercetin’s mechanism of action is not exclusively determined by modulation of the channel activity.<br />
|keywords=Epithelium, mitoBKCa channel, Mitochondria, Particulate matter, Quercetin<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Tsouka_2024_Commun_Med_(Lond)&diff=246485Tsouka 2024 Commun Med (Lond)2024-03-13T12:12:48Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Tsouka S, Kumar P, Seubnooch P, Freiburghaus K, St-Pierre M, Dufour JF, Masoodi M (2024) Transcriptomics-driven metabolic pathway analysis reveals similar alterations in lipid metabolism in mouse MASH model and human. Commun Med (Lond) 4:39. https://doi.org/10.1038/s43856-024-00465-3<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38443644 PMID: 38443644 Open Access]<br />
|authors=Tsouka Sofia, Kumar Pavitra, Seubnooch Patcharamon, Freiburghaus Katrin, St-Pierre Marie, Dufour Jean-Francois, Masoodi Mojgan<br />
|year=2024<br />
|journal=Commun Med (Lond)<br />
|abstract=Metabolic dysfunction-associated steatotic liver disease (MASLD) is a prevalent chronic liver disease worldwide, and can rapidly progress to metabolic dysfunction-associated steatohepatitis (MASH). Accurate preclinical models and methodologies are needed to understand underlying metabolic mechanisms and develop treatment strategies. Through meta-analysis of currently proposed mouse models, we hypothesized that a diet- and chemical-induced MASH model closely resembles the observed lipid metabolism alterations in humans.<br />
<br />
We developed transcriptomics-driven metabolic pathway analysis (TDMPA), a method to aid in the evaluation of metabolic resemblance. TDMPA uses genome-scale metabolic models to calculate enzymatic reaction perturbations from gene expression data. We performed TDMPA to score and compare metabolic pathway alterations in MASH mouse models to human MASH signatures. We used an already-established WD+CCl4-induced MASH model and performed functional assays and lipidomics to confirm TDMPA findings.<br />
<br />
Both human MASH and mouse models exhibit numerous altered metabolic pathways, including triglyceride biosynthesis, fatty acid beta-oxidation, bile acid biosynthesis, cholesterol metabolism, and oxidative phosphorylation. We confirm a significant reduction in mitochondrial functions and bioenergetics, as well as in acylcarnitines for the mouse model. We identify a wide range of lipid species within the most perturbed pathways predicted by TDMPA. Triglycerides, phospholipids, and bile acids are increased significantly in mouse MASH liver, confirming our initial observations.<br />
<br />
We introduce TDMPA, a methodology for evaluating metabolic pathway alterations in metabolic disorders. By comparing metabolic signatures that typify human MASH, we show a good metabolic resemblance of the WD+CCl4 mouse model. Our presented approach provides a valuable tool for defining metabolic space to aid experimental design for assessing metabolism.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration, Instruments;methods<br />
|diseases=Other<br />
|organism=Mouse<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS, ET<br />
|pathways=N, S, CIV, NS, ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Tsouka_2024_Commun_Med_(Lond)&diff=246478Tsouka 2024 Commun Med (Lond)2024-03-12T15:03:21Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Tsouka S, Kumar P, Seubnooch P, Freiburghaus K, St-Pierre M, Dufour JF, Masoodi M (2024) Transcriptomics-driven metabolic pathway analysis reveals similar alterations in lipid metabolism in mouse MASH model and human. Commun Med (Lond) 4:39. https://doi.org/10.1038/s43856-024-00465-3<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38443644 PMID: 38443644 Open Access]<br />
|authors=Tsouka Sofia, Kumar Pavitra, Seubnooch Patcharamon, Freiburghaus Katrin, St-Pierre Marie, Dufour Jean-Francois, Masoodi Mojgan<br />
|year=2024<br />
|journal=Commun Med (Lond)<br />
|abstract=Metabolic dysfunction-associated steatotic liver disease (MASLD) is a prevalent chronic liver disease worldwide, and can rapidly progress to metabolic dysfunction-associated steatohepatitis (MASH). Accurate preclinical models and methodologies are needed to understand underlying metabolic mechanisms and develop treatment strategies. Through meta-analysis of currently proposed mouse models, we hypothesized that a diet- and chemical-induced MASH model closely resembles the observed lipid metabolism alterations in humans.<br />
<br />
We developed transcriptomics-driven metabolic pathway analysis (TDMPA), a method to aid in the evaluation of metabolic resemblance. TDMPA uses genome-scale metabolic models to calculate enzymatic reaction perturbations from gene expression data. We performed TDMPA to score and compare metabolic pathway alterations in MASH mouse models to human MASH signatures. We used an already-established WD+CCl4-induced MASH model and performed functional assays and lipidomics to confirm TDMPA findings.<br />
<br />
Both human MASH and mouse models exhibit numerous altered metabolic pathways, including triglyceride biosynthesis, fatty acid beta-oxidation, bile acid biosynthesis, cholesterol metabolism, and oxidative phosphorylation. We confirm a significant reduction in mitochondrial functions and bioenergetics, as well as in acylcarnitines for the mouse model. We identify a wide range of lipid species within the most perturbed pathways predicted by TDMPA. Triglycerides, phospholipids, and bile acids are increased significantly in mouse MASH liver, confirming our initial observations.<br />
<br />
We introduce TDMPA, a methodology for evaluating metabolic pathway alterations in metabolic disorders. By comparing metabolic signatures that typify human MASH, we show a good metabolic resemblance of the WD+CCl4 mouse model. Our presented approach provides a valuable tool for defining metabolic space to aid experimental design for assessing metabolism.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Mouse<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS, ET<br />
|pathways=N, S, CIV, NS, ROX<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Commun_Med_(Lond)&diff=246477Commun Med (Lond)2024-03-12T14:43:39Z<p>Plangger Mario: Created page with "{{Journal |Title=[https://www.nature.com/commsmed Communications Medicine] }}"</p>
<hr />
<div>{{Journal<br />
|Title=[https://www.nature.com/commsmed Communications Medicine]<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Tsouka_2024_Commun_Med_(Lond)&diff=246476Tsouka 2024 Commun Med (Lond)2024-03-12T14:41:58Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Tsouka S, Kumar P, Seubnooch P, Freiburghaus K, St-Pierre M, Dufour JF, Masoodi M (2024) Transcriptomics-driven metabolic pathway analysis reveals similar alterations in lipid metabolism in mouse MASH model and human. Commun Med (Lond) 4:39. https://doi.org/10.1038/s43856-024-00465-3<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38443644 PMID: 38443644 Open Access]<br />
|authors=Tsouka Sofia, Kumar Pavitra, Seubnooch Patcharamon, Freiburghaus Katrin, St-Pierre Marie, Dufour Jean-Francois, Masoodi Mojgan<br />
|year=2024<br />
|journal=Commun Med (Lond)<br />
|abstract=Metabolic dysfunction-associated steatotic liver disease (MASLD) is a prevalent chronic liver disease worldwide, and can rapidly progress to metabolic dysfunction-associated steatohepatitis (MASH). Accurate preclinical models and methodologies are needed to understand underlying metabolic mechanisms and develop treatment strategies. Through meta-analysis of currently proposed mouse models, we hypothesized that a diet- and chemical-induced MASH model closely resembles the observed lipid metabolism alterations in humans.<br />
<br />
We developed transcriptomics-driven metabolic pathway analysis (TDMPA), a method to aid in the evaluation of metabolic resemblance. TDMPA uses genome-scale metabolic models to calculate enzymatic reaction perturbations from gene expression data. We performed TDMPA to score and compare metabolic pathway alterations in MASH mouse models to human MASH signatures. We used an already-established WD+CCl4-induced MASH model and performed functional assays and lipidomics to confirm TDMPA findings.<br />
<br />
Both human MASH and mouse models exhibit numerous altered metabolic pathways, including triglyceride biosynthesis, fatty acid beta-oxidation, bile acid biosynthesis, cholesterol metabolism, and oxidative phosphorylation. We confirm a significant reduction in mitochondrial functions and bioenergetics, as well as in acylcarnitines for the mouse model. We identify a wide range of lipid species within the most perturbed pathways predicted by TDMPA. Triglycerides, phospholipids, and bile acids are increased significantly in mouse MASH liver, confirming our initial observations.<br />
<br />
We introduce TDMPA, a methodology for evaluating metabolic pathway alterations in metabolic disorders. By comparing metabolic signatures that typify human MASH, we show a good metabolic resemblance of the WD+CCl4 mouse model. Our presented approach provides a valuable tool for defining metabolic space to aid experimental design for assessing metabolism.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Tsouka_2024_Commun_Med_(Lond)&diff=246475Tsouka 2024 Commun Med (Lond)2024-03-12T14:09:19Z<p>Plangger Mario: Created page with "{{Publication |title=Tsouka S, Kumar P, Seubnooch P, Freiburghaus K, St-Pierre M, Dufour JF, Masoodi M (2024) Transcriptomics-driven metabolic pathway analysis reveals similar..."</p>
<hr />
<div>{{Publication<br />
|title=Tsouka S, Kumar P, Seubnooch P, Freiburghaus K, St-Pierre M, Dufour JF, Masoodi M (2024) Transcriptomics-driven metabolic pathway analysis reveals similar alterations in lipid metabolism in mouse MASH model and human. Commun Med (Lond) 4:39. https://doi.org/10.1038/s43856-024-00465-3<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38443644 PMID: 38443644 Open Access]<br />
|authors=Tsouka S, Kumar P, Seubnooch P, Freiburghaus K, St-Pierre M, Dufour JF, Masoodi M<br />
|year=2024<br />
|journal=Commun Med (Lond)<br />
|abstract=Metabolic dysfunction-associated steatotic liver disease (MASLD) is a prevalent chronic liver disease worldwide, and can rapidly progress to metabolic dysfunction-associated steatohepatitis (MASH). Accurate preclinical models and methodologies are needed to understand underlying metabolic mechanisms and develop treatment strategies. Through meta-analysis of currently proposed mouse models, we hypothesized that a diet- and chemical-induced MASH model closely resembles the observed lipid metabolism alterations in humans.<br />
<br />
We developed transcriptomics-driven metabolic pathway analysis (TDMPA), a method to aid in the evaluation of metabolic resemblance. TDMPA uses genome-scale metabolic models to calculate enzymatic reaction perturbations from gene expression data. We performed TDMPA to score and compare metabolic pathway alterations in MASH mouse models to human MASH signatures. We used an already-established WD+CCl4-induced MASH model and performed functional assays and lipidomics to confirm TDMPA findings.<br />
<br />
Both human MASH and mouse models exhibit numerous altered metabolic pathways, including triglyceride biosynthesis, fatty acid beta-oxidation, bile acid biosynthesis, cholesterol metabolism, and oxidative phosphorylation. We confirm a significant reduction in mitochondrial functions and bioenergetics, as well as in acylcarnitines for the mouse model. We identify a wide range of lipid species within the most perturbed pathways predicted by TDMPA. Triglycerides, phospholipids, and bile acids are increased significantly in mouse MASH liver, confirming our initial observations.<br />
<br />
We introduce TDMPA, a methodology for evaluating metabolic pathway alterations in metabolic disorders. By comparing metabolic signatures that typify human MASH, we show a good metabolic resemblance of the WD+CCl4 mouse model. Our presented approach provides a valuable tool for defining metabolic space to aid experimental design for assessing metabolism.<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Halling_Jens_Frey&diff=246474Halling Jens Frey2024-03-12T13:43:13Z<p>Plangger Mario: Redirected page to Halling JF</p>
<hr />
<div>#REDIRECT[[Halling JF]]</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=DK_Copenhagen_Larsen_S&diff=246473DK Copenhagen Larsen S2024-03-12T13:42:45Z<p>Plangger Mario: </p>
<hr />
<div>{{O2k-Network Lab<br />
|institution=University of CopenhagenCenter for Healthy AgingFaculty Of Health SciencesDepartment of Biomedical Sciences<br />
|address=Blegdamsvej 3B<br />
|area code=DK-2200<br />
|city=Copenhagen<br />
|country=Denmark<br />
|weblink=[https://bmi.ku.dk/english/research/exercise-and-muscle/larsen-group/ Larsen Group – University of Copenhagen (ku.dk)]<br />
|Contact=Larsen Steen<br />
|MiPNetLab=Blom Ida, Bundgaard Fals Emma, Ahmt Petersen Emilie, Andersen Michelle, Helge Joern W, Halling Jens Frey, Kjaer Lange Kristine <br />
|Team previous=Boushel Robert C, Skovbro Mette, Hey-Mogensen Martin, Yokota Takashi, Gram Jensen M, Bach Jeppe, Beck Thomas, Dela Flemming, Dohlmann Tine, Helge Joern W, Kraunsoee Regitze, Lindemose Soeren, Neigaard-Hansen C, Soendergaard Stine, Taulo Lund M, Rodriguez-Juarez F, Rabol Rasmus, Stride Nis, Lundby Stine<br />
|Status=[[Power-O2k|''' 14 Power-O2k''']] 2018- ; previous: [[DK Copenhagen Dela F]]<br />
|info=[[MitoEAGLE Obergurgl 2019-01-31| MitoEAGLE 2019]], [[IOC116 | IOC116]], [[IOC109]], [[IOC95]], [[MiP2014]], [[IOC90]], [[IOC84]], [[IOC79]], [[MiP2013]], [[MiPschool Copenhagen DK 2013|MiPschool 2013]], [[IOC75]], [[IOC74]], [[Bioblast 2012 | Bioblast 2012]], [[MiP2011]], [[IOC61]], [[MiPNet15.07 IOC59|IOC59]], [[MiP2010|MiP2010]], [[MiPNet14.04 IOC51|IOC51]], [[MiPNet13.04 IOC47|IOC47]], [[MiPNet12.14 IOC39 | IOC39]], [[IOC36]], [[IOC31]], [[IOC30]], [[MiPNet10.09 MiP2005| MiP2005]], [[IOC28]], [[IOC26]], [[IOC24]], [[MiPNet08.10 MiP2003| MiP2003]]<br />
|Field_of_interest=Human muscle biopsies, healthy aging<br />
|keywords=Human muscle biopsies<br />
|Info=[http://www.oroboros.at/index.php?dela_f DK Copenhagen DelaF]<br />
}}<br />
== O2k-Feedback ==<br />
* ''The perspectives of working with the Oroboros Oxygraph-2k on human tissue are enormous'' Flemming Dela (2005).<br />
<br />
[[Category:Power-O2k]]</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=DK_Copenhagen_Larsen_S&diff=246472DK Copenhagen Larsen S2024-03-12T13:41:33Z<p>Plangger Mario: </p>
<hr />
<div>{{O2k-Network Lab<br />
|institution=University of CopenhagenCenter for Healthy AgingFaculty Of Health SciencesDepartment of Biomedical Sciences<br />
|address=Blegdamsvej 3B<br />
|area code=DK-2200<br />
|city=Copenhagen<br />
|country=Denmark<br />
|weblink=[https://bmi.ku.dk/english/research/exercise-and-muscle/larsen-group/ Larsen Group – University of Copenhagen (ku.dk)]<br />
|Contact=Larsen Steen<br />
|MiPNetLab=Blom Ida, Bundgaard Fals Emma, Ahmt Petersen Emilie, Andersen Michelle, Helge Joern W, Frey Halling Jens , Kjaer Lange Kristine <br />
|Team previous=Boushel Robert C, Skovbro Mette, Hey-Mogensen Martin, Yokota Takashi, Gram Jensen M, Bach Jeppe, Beck Thomas, Dela Flemming, Dohlmann Tine, Helge Joern W, Kraunsoee Regitze, Lindemose Soeren, Neigaard-Hansen C, Soendergaard Stine, Taulo Lund M, Rodriguez-Juarez F, Rabol Rasmus, Stride Nis, Lundby Stine<br />
|Status=[[Power-O2k|''' 14 Power-O2k''']] 2018- ; previous: [[DK Copenhagen Dela F]]<br />
|info=[[MitoEAGLE Obergurgl 2019-01-31| MitoEAGLE 2019]], [[IOC116 | IOC116]], [[IOC109]], [[IOC95]], [[MiP2014]], [[IOC90]], [[IOC84]], [[IOC79]], [[MiP2013]], [[MiPschool Copenhagen DK 2013|MiPschool 2013]], [[IOC75]], [[IOC74]], [[Bioblast 2012 | Bioblast 2012]], [[MiP2011]], [[IOC61]], [[MiPNet15.07 IOC59|IOC59]], [[MiP2010|MiP2010]], [[MiPNet14.04 IOC51|IOC51]], [[MiPNet13.04 IOC47|IOC47]], [[MiPNet12.14 IOC39 | IOC39]], [[IOC36]], [[IOC31]], [[IOC30]], [[MiPNet10.09 MiP2005| MiP2005]], [[IOC28]], [[IOC26]], [[IOC24]], [[MiPNet08.10 MiP2003| MiP2003]]<br />
|Field_of_interest=Human muscle biopsies, healthy aging<br />
|keywords=Human muscle biopsies<br />
|Info=[http://www.oroboros.at/index.php?dela_f DK Copenhagen DelaF]<br />
}}<br />
== O2k-Feedback ==<br />
* ''The perspectives of working with the Oroboros Oxygraph-2k on human tissue are enormous'' Flemming Dela (2005).<br />
<br />
[[Category:Power-O2k]]</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=DK_Copenhagen_Larsen_S&diff=246470DK Copenhagen Larsen S2024-03-12T13:06:47Z<p>Plangger Mario: </p>
<hr />
<div>{{O2k-Network Lab<br />
|institution=University of CopenhagenCenter for Healthy AgingFaculty Of Health SciencesDepartment of Biomedical Sciences<br />
|address=Blegdamsvej 3B<br />
|area code=DK-2200<br />
|city=Copenhagen<br />
|country=Denmark<br />
|weblink=[https://bmi.ku.dk/english/research/exercise-and-muscle/larsen-group/ Larsen Group – University of Copenhagen (ku.dk)]<br />
|Contact=Larsen Steen<br />
|MiPNetLab=Bach Jeppe, Beck Thomas, Dela Flemming, Dohlmann Tine, Helge Joern W, Kraunsoee Regitze, Lindemose Soeren, Neigaard-Hansen C, Soendergaard Stine, Taulo Lund M, Rodriguez-Juarez F, Rabol Rasmus, Stride Nis, Lundby Stine<br />
|Team previous=Boushel Robert C, Skovbro Mette, Hey-Mogensen Martin, Yokota Takashi, Gram Jensen M<br />
|Status=[[Power-O2k|''' 14 Power-O2k''']] 2018- ; previous: [[DK Copenhagen Dela F]]<br />
|info=[[MitoEAGLE Obergurgl 2019-01-31| MitoEAGLE 2019]], [[IOC116 | IOC116]], [[IOC109]], [[IOC95]], [[MiP2014]], [[IOC90]], [[IOC84]], [[IOC79]], [[MiP2013]], [[MiPschool Copenhagen DK 2013|MiPschool 2013]], [[IOC75]], [[IOC74]], [[Bioblast 2012 | Bioblast 2012]], [[MiP2011]], [[IOC61]], [[MiPNet15.07 IOC59|IOC59]], [[MiP2010|MiP2010]], [[MiPNet14.04 IOC51|IOC51]], [[MiPNet13.04 IOC47|IOC47]], [[MiPNet12.14 IOC39 | IOC39]], [[IOC36]], [[IOC31]], [[IOC30]], [[MiPNet10.09 MiP2005| MiP2005]], [[IOC28]], [[IOC26]], [[IOC24]], [[MiPNet08.10 MiP2003| MiP2003]]<br />
|Field_of_interest=Human muscle biopsies, healthy aging<br />
|keywords=Human muscle biopsies<br />
|Info=[http://www.oroboros.at/index.php?dela_f DK Copenhagen DelaF]<br />
}}<br />
== O2k-Feedback ==<br />
* ''The perspectives of working with the Oroboros Oxygraph-2k on human tissue are enormous'' Flemming Dela (2005).<br />
<br />
[[Category:Power-O2k]]</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=J_Exerc_Rehabil&diff=246440J Exerc Rehabil2024-03-11T15:47:54Z<p>Plangger Mario: Created page with "{{Journal |Title=[https://www.e-jer.org/ Journal of Exercise Rehabilitation] }}"</p>
<hr />
<div>{{Journal<br />
|Title=[https://www.e-jer.org/ Journal of Exercise Rehabilitation]<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kim_2024_J_Exerc_Rehabil&diff=246439Kim 2024 J Exerc Rehabil2024-03-11T15:47:18Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kim TW, Park SS, Kim SH, Kim MK, Shin MS, Kim SH (2024) Exercise before pregnancy exerts protective effect on prenatal stress-induced impairment of memory, neurogenesis, and mitochondrial function in offspring. J Exerc Rehabil 20:2-10. https://doi.org/10.12965/jer.2448068.034<br />
|info=[https://www.ncbi.nlm.nih.gov/pubmed/38433854 PMID: 38433854 Open Access]<br />
|authors=Kim Tae-Woon, Park Sang-Seo, Kim Sang-Hoon, Kim Myung-Ki, Shin Mal-Soon, Kim Seong-Hyun<br />
|year=2024<br />
|journal=J Exerc Rehabil<br />
|abstract=Stress during pregnancy has a negative effect on the fetus. However, maternal exercise has a positive effect on the cognitive function of the fetus and alleviates the negative effects of stress. This study aimed to demonstrate whether exercise before pregnancy has a protective effect on prenatal stress-induced impairment of memory, neurogenesis and mitochondrial function in mice offspring. In this experiment, immunohistochemistry, Western blot, measurement of mitochondria oxygen respiration, and behavior tests were performed. Spatial memory and short-term memory of the offspring from the prenatal stress with exercise were increased compared to the offspring from the prenatal stress. The numbers of doublecortin-positive and 5-bromo-2'-deoxyuridine-positive cells in the hippocampal dentate gyrus of the offspring from the prenatal stress with exercise were higher compared to the offspring from the prenatal stress. The expressions of brain-derived neurotrophic factor, postsynaptic density 95 kDa, and synaptophysin in the hippocampus of the offspring from the prenatal stress with exercise were enhanced compared to the offspring from the prenatal stress. Oxygen consumption of the offspring from the prenatal stress with exercise were higher compared to the offspring from the prenatal stress. Exercise before pregnancy alleviated prenatal stress-induced impairment of memory, neurogenesis, and mitochondrial function. Therefore, exercise before pregnancy may have a protective effect against prenatal stress of the offspring.<br />
|keywords=Exercise, Maternal stress, Memory, Offspring, Pregnancy<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration, Exercise physiology;nutrition;life style<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kim_2024_J_Exerc_Rehabil&diff=246438Kim 2024 J Exerc Rehabil2024-03-11T15:46:39Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Kim TW, Park SS, Kim SH, Kim MK, Shin MS, Kim SH (2024) Exercise before pregnancy exerts protective effect on prenatal stress-induced impairment of memory, neurogenesis, and mitochondrial function in offspring. J Exerc Rehabil 20:2-10. https://doi.org/10.12965/jer.2448068.034<br />
|info=[https://www.ncbi.nlm.nih.gov/pubmed/38433854 PMID: 38433854 Open Access]<br />
|authors=Kim Tae-Woon, Park Sang-Seo, Kim Sang-Hoon, Kim Myung-Ki, Shin Mal-Soon, Kim Seong-Hyun<br />
|year=2024<br />
|journal=J Exerc Rehabil<br />
|abstract=Stress during pregnancy has a negative effect on the fetus. However, maternal exercise has a positive effect on the cognitive function of the fetus and alleviates the negative effects of stress. This study aimed to demonstrate whether exercise before pregnancy has a protective effect on prenatal stress-induced impairment of memory, neurogenesis and mitochondrial function in mice offspring. In this experiment, immunohistochemistry, Western blot, measurement of mitochondria oxygen respiration, and behavior tests were performed. Spatial memory and short-term memory of the offspring from the prenatal stress with exercise were increased compared to the offspring from the prenatal stress. The numbers of doublecortin-positive and 5-bromo-2'-deoxyuridine-positive cells in the hippocampal dentate gyrus of the offspring from the prenatal stress with exercise were higher compared to the offspring from the prenatal stress. The expressions of brain-derived neurotrophic factor, postsynaptic density 95 kDa, and synaptophysin in the hippocampus of the offspring from the prenatal stress with exercise were enhanced compared to the offspring from the prenatal stress. Oxygen consumption of the offspring from the prenatal stress with exercise were higher compared to the offspring from the prenatal stress. Exercise before pregnancy alleviated prenatal stress-induced impairment of memory, neurogenesis, and mitochondrial function. Therefore, exercise before pregnancy may have a protective effect against prenatal stress of the offspring.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Kim_2024_J_Exerc_Rehabil&diff=246434Kim 2024 J Exerc Rehabil2024-03-11T15:26:33Z<p>Plangger Mario: Created page with "{{Publication |title=Kim TW, Park SS, Kim SH, Kim MK, Shin MS, Kim SH (2024) Exercise before pregnancy exerts protective effect on prenatal stress-induced impairment of memory..."</p>
<hr />
<div>{{Publication<br />
|title=Kim TW, Park SS, Kim SH, Kim MK, Shin MS, Kim SH (2024) Exercise before pregnancy exerts protective effect on prenatal stress-induced impairment of memory, neurogenesis, and mitochondrial function in offspring. J Exerc Rehabil 20:2-10. https://doi.org/10.12965/jer.2448068.034<br />
|info=[https://www.ncbi.nlm.nih.gov/pubmed/38433854 PMID: 38433854 Open Access]<br />
|authors=Kim TW, Park SS, Kim SH, Kim MK, Shin MS, Kim SH<br />
|year=2024<br />
|journal=J Exerc Rehabil<br />
|abstract=Stress during pregnancy has a negative effect on the fetus. However, maternal exercise has a positive effect on the cognitive function of the fetus and alleviates the negative effects of stress. This study aimed to demonstrate whether exercise before pregnancy has a protective effect on prenatal stress-induced impairment of memory, neurogenesis and mitochondrial function in mice offspring. In this experiment, immunohistochemistry, Western blot, measurement of mitochondria oxygen respiration, and behavior tests were performed. Spatial memory and short-term memory of the offspring from the prenatal stress with exercise were increased compared to the offspring from the prenatal stress. The numbers of doublecortin-positive and 5-bromo-2'-deoxyuridine-positive cells in the hippocampal dentate gyrus of the offspring from the prenatal stress with exercise were higher compared to the offspring from the prenatal stress. The expressions of brain-derived neurotrophic factor, postsynaptic density 95 kDa, and synaptophysin in the hippocampus of the offspring from the prenatal stress with exercise were enhanced compared to the offspring from the prenatal stress. Oxygen consumption of the offspring from the prenatal stress with exercise were higher compared to the offspring from the prenatal stress. Exercise before pregnancy alleviated prenatal stress-induced impairment of memory, neurogenesis, and mitochondrial function. Therefore, exercise before pregnancy may have a protective effect against prenatal stress of the offspring.<br />
|editor=[[Plangger M]]<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Taylor_2024_Pilot_Feasibility_Stud&diff=246401Taylor 2024 Pilot Feasibility Stud2024-03-07T14:03:15Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Taylor MK, Burns JM, Choi IY, Herda TJ, Lee P, Smith AN, Sullivan DK, Swerdlow RH, Wilkins HM (2024) Protocol for a single-arm, pilot trial of creatine monohydrate supplementation in patients with Alzheimer's disease. Pilot Feasibility Stud 10:42. https://doi.org/10.1186/s40814-024-01469-5<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38414003 PMID: 38414003 Open Access]<br />
|authors=Taylor Matthew K, Burns Jeffrey M, Choi In-Young, Herda Trent J, Lee Phil, Smith Aaron N, Sullivan Debra K, Swerdlow Russell H, Wilkins Heather M<br />
|year=2024<br />
|journal=Pilot Feasibility Stud<br />
|abstract=Impaired brain bioenergetics is a pathological hallmark of Alzheimer's disease (AD) and is a compelling target for AD treatment. Patients with AD exhibit dysfunction in the brain creatine (Cr) system, which is integral in maintaining bioenergetic flux. Recent studies in AD mouse models suggest Cr supplementation improves brain mitochondrial function and may be protective of AD peptide pathology and cognition.<br />
<br />
The Creatine to Augment Bioenergetics in Alzheimer's disease (CABA) study is designed to primarily assess the feasibility of supplementation with 20 g/day of creatine monohydrate (CrM) in patients with cognitive impairment due to AD. Secondary aims are designed to generate preliminary data investigating changes in brain Cr levels, cognition, peripheral and brain mitochondrial function, and muscle strength and size.<br />
<br />
CABA is an 8-week, single-arm pilot study that will recruit 20 patients with cognitive impairment due to AD. Participants attend five in-person study visits: two visits at baseline to conduct screening and baseline assessments, a 4-week visit, and two 8-week visits. Outcomes assessment includes recruitment, retention, and compliance, cognitive testing, magnetic resonance spectroscopy of brain metabolites, platelet and lymphocyte mitochondrial function, and muscle strength and morphology at baseline and 8 weeks.<br />
<br />
CABA is the first study to investigate CrM as a potential treatment in patients with AD. The pilot data generated by this study are pertinent to inform the design of future large-scale efficacy trials.<br />
|keywords=Alzheimer’s disease, Bioenergetics, Brain, Creatine, Pilot trial<br />
|editor=[[Plangger M]]<br />
|mipnetlab=US KS Kansas City Swerdlow RH, US KS Kansas City Wilkins H<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|diseases=Alzheimer's<br />
|organism=Human<br />
|tissues=Lymphocyte, Platelet<br />
|preparations=Permeabilized cells<br />
|instruments=Oxygraph-2k, O2k-Fluorometer<br />
|additional=2024-03<br />
}}</div>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Taylor_2024_Pilot_Feasibility_Stud&diff=246400Taylor 2024 Pilot Feasibility Stud2024-03-07T14:00:33Z<p>Plangger Mario: </p>
<hr />
<div>{{Publication<br />
|title=Taylor MK, Burns JM, Choi IY, Herda TJ, Lee P, Smith AN, Sullivan DK, Swerdlow RH, Wilkins HM (2024) Protocol for a single-arm, pilot trial of creatine monohydrate supplementation in patients with Alzheimer's disease. Pilot Feasibility Stud 10:42. https://doi.org/10.1186/s40814-024-01469-5<br />
|info=[https://pubmed.ncbi.nlm.nih.gov/38414003 PMID: 38414003 Open Access]<br />
|authors=Taylor Matthew K, Burns Jeffrey M, Choi In-Young, Herda Trent J, Lee Phil, Smith Aaron N, Sullivan Debra K, Swerdlow Russell H, Wilkins Heather M<br />
|year=2024<br />
|journal=Pilot Feasibility Stud<br />
|abstract=Impaired brain bioenergetics is a pathological hallmark of Alzheimer's disease (AD) and is a compelling target for AD treatment. Patients with AD exhibit dysfunction in the brain creatine (Cr) system, which is integral in maintaining bioenergetic flux. Recent studies in AD mouse models suggest Cr supplementation improves brain mitochondrial function and may be protective of AD peptide pathology and cognition.<br />
<br />
The Creatine to Augment Bioenergetics in Alzheimer's disease (CABA) study is designed to primarily assess the feasibility of supplementation with 20 g/day of creatine monohydrate (CrM) in patients with cognitive impairment due to AD. Secondary aims are designed to generate preliminary data investigating changes in brain Cr levels, cognition, peripheral and brain mitochondrial function, and muscle strength and size.<br />
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CABA is an 8-week, single-arm pilot study that will recruit 20 patients with cognitive impairment due to AD. Participants attend five in-person study visits: two visits at baseline to conduct screening and baseline assessments, a 4-week visit, and two 8-week visits. Outcomes assessment includes recruitment, retention, and compliance, cognitive testing, magnetic resonance spectroscopy of brain metabolites, platelet and lymphocyte mitochondrial function, and muscle strength and morphology at baseline and 8 weeks.<br />
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CABA is the first study to investigate CrM as a potential treatment in patients with AD. The pilot data generated by this study are pertinent to inform the design of future large-scale efficacy trials.<br />
|keywords=Alzheimer’s disease, Bioenergetics, Brain, Creatine, Pilot trial<br />
|editor=[[Plangger M]]<br />
|mipnetlab=US KS Kansas City Swerdlow RH, US KS Kansas City Wilkins H<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|instruments=Oxygraph-2k<br />
|additional=2024-03<br />
}}</div>Plangger Mario