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Garedew 2006 Biochim Biophys Acta - Revision history
2024-03-29T10:16:53Z
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Gnaiger Erich at 16:14, 10 January 2022
2022-01-10T16:14:37Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 16:14, 10 January 2022</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in Oroboros O2k instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in Oroboros O2k instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=<del style="font-weight: bold; text-decoration: none;">AT_Innsbruck_Gnaiger E</del>, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=<ins style="font-weight: bold; text-decoration: none;">AT Innsbruck Oroboros</ins>, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
</table>
Gnaiger Erich
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=170797&oldid=prev
Beno Marija at 07:47, 23 January 2019
2019-01-23T07:47:50Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 07:47, 23 January 2019</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in <del style="font-weight: bold; text-decoration: none;">OROBOROS </del>O2k instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in <ins style="font-weight: bold; text-decoration: none;">Oroboros </ins>O2k instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=AT_Innsbruck_Gnaiger E, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=AT_Innsbruck_Gnaiger E, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td></tr>
</table>
Beno Marija
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=123440&oldid=prev
Beno Marija at 14:38, 7 November 2016
2016-11-07T14:38:53Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:38, 7 November 2016</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del style="font-weight: bold; text-decoration: none;">substratestates</del>=<del style="font-weight: bold; text-decoration: none;">CI</del>, <del style="font-weight: bold; text-decoration: none;">CII</del>, <del style="font-weight: bold; text-decoration: none;">CI&II</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins style="font-weight: bold; text-decoration: none;">pathways</ins>=<ins style="font-weight: bold; text-decoration: none;">N</ins>, <ins style="font-weight: bold; text-decoration: none;">S</ins>, <ins style="font-weight: bold; text-decoration: none;">NS</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
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Beno Marija
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=88787&oldid=prev
Went Nora at 09:12, 13 May 2015
2015-05-13T09:12:48Z
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in OROBOROS <del style="font-weight: bold; text-decoration: none;">Oxygraph-2k </del>instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in OROBOROS <ins style="font-weight: bold; text-decoration: none;">O2k </ins>instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=AT_Innsbruck_Gnaiger E, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=AT_Innsbruck_Gnaiger E, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td></tr>
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</table>
Went Nora
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=79572&oldid=prev
Marte Verena at 14:47, 10 February 2015
2015-02-10T14:47:15Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:47, 10 February 2015</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Abstract</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Abstract</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|title=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E (2006) High excess capacity of cytochrome ''c'' oxidase in permeabilized fibers of the mouse heart. Biochim Biophys Acta, EBEC Short Reports Suppl 14 (2006): 167-<del style="font-weight: bold; text-decoration: none;">168</del>.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|title=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E (2006) High excess capacity of cytochrome ''c'' oxidase in permeabilized fibers of the mouse heart. Biochim Biophys Acta, EBEC Short Reports Suppl 14 (2006):167-<ins style="font-weight: bold; text-decoration: none;">8</ins>.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.oroboros.at/index.php?id=gnaiger-bba-2006 Weblink]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.oroboros.at/index.php?id=gnaiger-bba-2006 Weblink]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Heart</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Heart</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Enzyme, Oxidase; <del style="font-weight: bold; text-decoration: none;">Biochemical Oxidation</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Enzyme, Oxidase;<ins style="font-weight: bold; text-decoration: none;">biochemical oxidation</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|topics=Flux control, Inhibitor, Threshold;excess capacity</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|topics=Flux control, Inhibitor, Threshold;excess capacity</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|substratestates=CI, CII, CI<del style="font-weight: bold; text-decoration: none;">+</del>II</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|substratestates=CI, CII, CI<ins style="font-weight: bold; text-decoration: none;">&</ins>II</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td></tr>
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</table>
Marte Verena
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=49581&oldid=prev
Gnaiger Erich at 22:23, 11 August 2013
2013-08-11T22:23:34Z
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Enzyme, Oxidase; Biochemical Oxidation</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Enzyme, Oxidase; Biochemical Oxidation</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|topics=Flux control, Inhibitor, Threshold; excess capacity</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|topics=Flux control, Inhibitor, Threshold;excess capacity</div></td></tr>
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Gnaiger Erich
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=48987&oldid=prev
Gnaiger Erich at 11:19, 11 August 2013
2013-08-11T11:19:19Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 11:19, 11 August 2013</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Abstract</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Abstract</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|title=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E (2006) High excess capacity of cytochrome c oxidase in permeabilized fibers of the mouse heart. Biochim Biophys Acta, EBEC Short Reports Suppl 14 (2006): 167-168.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|title=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E (2006) High excess capacity of cytochrome <ins style="font-weight: bold; text-decoration: none;">''</ins>c<ins style="font-weight: bold; text-decoration: none;">'' </ins>oxidase in permeabilized fibers of the mouse heart. Biochim Biophys Acta, EBEC Short Reports Suppl 14 (2006): 167-168.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.oroboros.at/index.php?id=gnaiger-bba-2006 Weblink]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[http://www.oroboros.at/index.php?id=gnaiger-bba-2006 Weblink]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Labeling</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Labeling</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del style="font-weight: bold; text-decoration: none;">instruments</del>=<del style="font-weight: bold; text-decoration: none;">Oxygraph-2k</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins style="font-weight: bold; text-decoration: none;">area</ins>=<ins style="font-weight: bold; text-decoration: none;">Respiration</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Mouse</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Mouse</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Heart</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Heart</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Oxidase; Biochemical Oxidation, <del style="font-weight: bold; text-decoration: none;">Enzyme</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue<ins style="font-weight: bold; text-decoration: none;">, Enzyme</ins>, Oxidase; Biochemical Oxidation</div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|topics=Flux control</ins>, <ins style="font-weight: bold; text-decoration: none;">Inhibitor, Threshold; excess capacity</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del style="font-weight: bold; text-decoration: none;">kinetics</del>=<del style="font-weight: bold; text-decoration: none;">Inhibitor; Uncoupler</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins style="font-weight: bold; text-decoration: none;">substratestates</ins>=<ins style="font-weight: bold; text-decoration: none;">CI, CII, CI+II</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|instruments=Oxygraph-2k</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|journal=Biochim Biophys Acta</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
</table>
Gnaiger Erich
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=43296&oldid=prev
Meissner Barbara at 09:31, 27 February 2013
2013-02-27T09:31:54Z
<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:31, 27 February 2013</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|instruments=Oxygraph-2k</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Mouse</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Mouse</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|tissues=<del style="font-weight: bold; text-decoration: none;">Cardiac muscle</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|tissues=<ins style="font-weight: bold; text-decoration: none;">Heart</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Oxidase; Biochemical Oxidation, Enzyme</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Oxidase; Biochemical Oxidation, Enzyme</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|couplingstates=OXPHOS</div></td></tr>
</table>
Meissner Barbara
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=36458&oldid=prev
Meissner Barbara at 12:47, 15 November 2012
2012-11-15T12:47:06Z
<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
<col class="diff-marker" />
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<col class="diff-marker" />
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<tr class="diff-title" lang="en">
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 12:47, 15 November 2012</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|authors=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2006</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">|journal=Biochim Biophys Acta</del></div></td><td colspan="2"></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in OROBOROS Oxygraph-2k instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=Metabolic flux control analysis and the concept of excess capacity of enzymes over pathway flux are related by the functional threshold, at which damage or inhibition of an enzyme reduces excess capacity to a minimum and starts to limit overall flux through the pathway. Excess capacity of cytochrome c oxidase (COX) varies between tissues, but little is known about differences between species. In particular, information is lacking on mitochondrial respiratory function in the mouse heart, despite the fact that transgenic mice provide increasingly important animal models. Permeabilized muscle fibers were prepared from the left ventricle of a single mouse heart, and measured in OROBOROS Oxygraph-2k instruments in parallel at 4, 25, 30, 37 and 40 °C (N³4). Threshold plots were constructed from azide titrations of flux through the electron transport chain (parallel e-input into complexes I+II with malate+pyruvate+glutamate+succinate and uncoupling by FCCP), versus COX (0.5 mM TMPD+2 mM ascorbate after uncoupling and inhibition by rotenone+malonate+antimycin A). Azide was used, since inhibition of COX by cyanide is reversed by pyruvate particularly at low oxygen levels. The inhibition constant, ''K''i, of COX for azide was 0.1 mM at 37 °C, increasing from 4 to 40 °C over two orders of magnitude. COX velocity measured with TMPD+ascorbate was 1.3-fold of maximum electron transport capacity of the respiratory chain at 25 to 40 °C, and 3.3-fold at 4 °C. In contrast, linear extrapolations of threshold plots revealed a COX excess capacity of 1.6-fold over pathway flux in the range of 30 to 40 °C, increasing to 1.8- and 7.6-fold at 25 °C and 4 °C, respectively. Application of complex I substrates only, would yield an apparent COX excess capacity of >3-fold over pathway flux (at 30 and 37 °C), since parallel e-input through complex I+II doubled flux compared to complex I substrates. Taken together, COX excess capacity in myocardial fibers of the mouse was significantly higher than in fibers of rat heart or human skeletal muscle. Results obtained under hypothermic incubation conditions of permeabilzed fibers may be extrapolated to physiological temperature of 37 °C with caution only. The very high COX excess capacity under hypothermia (4 °C) may compensate for hypothermic hypoxia by decreasing the p<sub>50</sub> of mitochondrial respiration in parallel to the decreased p<sub>50</sub> of hemoglobin and myoglobin. The present study yields an important baseline for further investigations of mitochondrial function in the mouse heart, including genetic models of acquired and inherited mitochondrial defects.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=AT_Innsbruck_Gnaiger E, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mipnetlab=AT_Innsbruck_Gnaiger E, CA_Rimouski_Blier PU, CA_Edmonton_Lemieux H</div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|journal=Biochim Biophys Acta</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Oxidase; Biochemical Oxidation, Enzyme</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|preparations=Permeabilized tissue, Oxidase; Biochemical Oxidation, Enzyme</div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|couplingstates=OXPHOS</ins></div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|<del style="font-weight: bold; text-decoration: none;">topics</del>=<del style="font-weight: bold; text-decoration: none;">Respiration; OXPHOS; ETS Capacity, Flux Control; Additivity; Threshold; Excess Capacity</del></div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|<ins style="font-weight: bold; text-decoration: none;">journal</ins>=<ins style="font-weight: bold; text-decoration: none;">Biochim Biophys Acta</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|discipline=Mitochondrial Physiology</div></td></tr>
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Meissner Barbara
https://wiki.oroboros.at/index.php?title=Garedew_2006_Biochim_Biophys_Acta&diff=27600&oldid=prev
Gnaiger Erich at 23:33, 4 April 2012
2012-04-04T23:33:30Z
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 23:33, 4 April 2012</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|title=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E (2006) High excess capacity of cytochrome c oxidase in permeabilized fibers of the mouse heart. Biochim Biophys Acta, EBEC Short Reports Suppl 14 (2006): 167-168.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|title=Garedew A, Lemieux H, Schachner T, Blier PU, Tardif J-C, Gnaiger E (2006) High excess capacity of cytochrome c oxidase in permeabilized fibers of the mouse heart. Biochim Biophys Acta, EBEC Short Reports Suppl 14 (2006): 167-168.</div></td></tr>
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Gnaiger Erich