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Difference between revisions of "Varikmaa 2014 Biochim Biophys Acta"

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{{Publication
{{Publication
|title=Varikmaa M, Bagur R, Kaambre T, Grichine A, Timohhina N, Tepp K, Shevchuk I, Chekulayev V, Metsis M, Boucher F, Saks V, Kuznetsov AV, Guzun R (2013) Role of mitochondria-cytoskeleton interactions in respiration regulation and mitochondrial organization in striated muscles. Biochim Biophys Acta 1837:232-45.
|title=Varikmaa M, Bagur R, Kaambre T, Grichine A, Timohhina N, Tepp K, Shevchuk I, Chekulayev V, Metsis M, Boucher F, Saks V, Kuznetsov AV, Guzun R (2014) Role of mitochondria-cytoskeleton interactions in respiration regulation and mitochondrial organization in striated muscles. Biochim Biophys Acta 1837:232-45.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/24189374 PMID: 24189374]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/24189374 PMID: 24189374]
|authors=Varikmaa M, Bagur R, Kaambre T, Grichine A, Timohhina N, Tepp K, Shevchuk I, Chekulayev V, Metsis M, Boucher F, Saks V, Kuznetsov AV, Guzun R
|authors=Varikmaa M, Bagur R, Kaambre T, Grichine A, Timohhina N, Tepp K, Shevchuk I, Chekulayev V, Metsis M, Boucher F, Saks V, Kuznetsov AV, Guzun R
|year=2014
|year=2014
|journal=Biochim Biophys Acta
|journal=Biochim Biophys Acta
|abstract=The aim of this work was to study the regulation of respiration and energy fluxes in permeabilized oxidative and glycolytic skeletal muscle fibers, focusing also on the role of cytoskeletal protein tubulin βII isotype in mitochondrial metabolism and organization. By analyzing accessibility of mitochondrial ADP, using respirometry and pyruvate kinase-phosphoenolpyruvate trapping system for ADP, we show that the apparent affinity of respiration for ADP can be directly linked to the permeability of the mitochondrial outer membrane (MOM). Previous studies have shown that MOM permeability in cardiomyocytes can be regulated by VDAC interaction with cytoskeletal protein, βII tubulin. We found that in oxidative soleus skeletal muscle the high apparent Km for ADP is associated with low MOM permeability and high expression of non-polymerized βII tubulin. Very low expression of non-polymerized form of βII tubulin in glycolytic muscles is associated with high MOM permeability for adenine nucleotides (low apparent Km for ADP).
|abstract=The aim of this work was to study the regulation of respiration and energy fluxes in permeabilized oxidative and glycolytic skeletal muscle fibers, focusing also on the role of cytoskeletal protein tubulin βII isotype in mitochondrial metabolism and organization. By analyzing accessibility of mitochondrial ADP, using respirometry and pyruvate kinase-phosphoenolpyruvate trapping system for ADP, we show that the apparent affinity of respiration for ADP can be directly linked to the permeability of the mitochondrial outer membrane (mtOM). Previous studies have shown that mtOM permeability in cardiomyocytes can be regulated by VDAC interaction with cytoskeletal protein, βII tubulin. We found that in oxidative soleus skeletal muscle the high apparent Km for ADP is associated with low mtOM permeability and high expression of non-polymerized βII tubulin. Very low expression of non-polymerized form of βII tubulin in glycolytic muscles is associated with high mtOM permeability for adenine nucleotides (low apparent Km for ADP).
|keywords=Energy flux, Intracellular energy unit, Metabolic control analysis, Respiration, Skeletal muscle
|keywords=Energy flux, Intracellular energy unit, Metabolic control analysis, Respiration, Skeletal muscle
|mipnetlab=EE Tallinn Kaambre T, FR Grenoble Saks VA, FR Grenoble Schlattner U
|mipnetlab=EE Tallinn Kaambre T, FR Grenoble Saks VA, FR Grenoble Schlattner U
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|topics=Inhibitor, PCr;Cr
|topics=Inhibitor, PCr;Cr
|couplingstates=LEAK, OXPHOS
|couplingstates=LEAK, OXPHOS
|substratestates=CI, CIII, CIV
|pathways=N, CIV
|instruments=Oxygraph-2k
|instruments=Oxygraph-2k
}}
}}

Latest revision as of 16:06, 19 October 2017

Publications in the MiPMap
Varikmaa M, Bagur R, Kaambre T, Grichine A, Timohhina N, Tepp K, Shevchuk I, Chekulayev V, Metsis M, Boucher F, Saks V, Kuznetsov AV, Guzun R (2014) Role of mitochondria-cytoskeleton interactions in respiration regulation and mitochondrial organization in striated muscles. Biochim Biophys Acta 1837:232-45.

» PMID: 24189374

Varikmaa M, Bagur R, Kaambre T, Grichine A, Timohhina N, Tepp K, Shevchuk I, Chekulayev V, Metsis M, Boucher F, Saks V, Kuznetsov AV, Guzun R (2014) Biochim Biophys Acta

Abstract: The aim of this work was to study the regulation of respiration and energy fluxes in permeabilized oxidative and glycolytic skeletal muscle fibers, focusing also on the role of cytoskeletal protein tubulin βII isotype in mitochondrial metabolism and organization. By analyzing accessibility of mitochondrial ADP, using respirometry and pyruvate kinase-phosphoenolpyruvate trapping system for ADP, we show that the apparent affinity of respiration for ADP can be directly linked to the permeability of the mitochondrial outer membrane (mtOM). Previous studies have shown that mtOM permeability in cardiomyocytes can be regulated by VDAC interaction with cytoskeletal protein, βII tubulin. We found that in oxidative soleus skeletal muscle the high apparent Km for ADP is associated with low mtOM permeability and high expression of non-polymerized βII tubulin. Very low expression of non-polymerized form of βII tubulin in glycolytic muscles is associated with high mtOM permeability for adenine nucleotides (low apparent Km for ADP). Keywords: Energy flux, Intracellular energy unit, Metabolic control analysis, Respiration, Skeletal muscle

O2k-Network Lab: EE Tallinn Kaambre T, FR Grenoble Saks VA, FR Grenoble Schlattner U


Labels: MiParea: Respiration, mt-Membrane, Comparative MiP;environmental MiP 


Organism: Rat  Tissue;cell: Heart, Skeletal muscle  Preparation: Permeabilized cells, Isolated mitochondria 

Regulation: Inhibitor, PCr;Cr  Coupling state: LEAK, OXPHOS  Pathway: N, CIV  HRR: Oxygraph-2k