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Difference between revisions of "Gueguen 2005 J Physiol"

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{{Publication
{{Publication
|title=Gueguen N, Lefaucheur L, Ecolan P, Fillaut M, Herpin P (2005) Ca2+-activated myosin-ATPases, creatine and adenylate kinases regulate mitochondrial function according to myofibre type in rabbit. J Physiol 564: 723-735.
|title=Gueguen N, Lefaucheur L, Ecolan P, Fillaut M, Herpin P (2005) Ca2+-activated myosin-ATPases, creatine and adenylate kinases regulate mitochondrial function according to myofibre type in rabbit. J Physiol 564:723-35.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/15731190 PMID: 15731190]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/15731190 PMID: 15731190 Open Access]
|authors=Gueguen N, Lefaucheur L, Ecolan P, Fillaut M, Herpin P
|authors=Gueguen N, Lefaucheur L, Ecolan P, Fillaut M, Herpin P
|year=2005
|year=2005
|journal=J Physiol
|journal=J Physiol
|abstract=Mitochondrial respiration rates and their regulation by ADP, AMP and creatine, were studied at different free Ca<sup>2+</sup>  concentrations (0.1 versus 0.4 μm) on permeabilized fibre bundles of rabbit skeletal muscles differing in their myosin heavy chain profiles. Four fibre bundle types were obtained: pure types I and IIx, and mixed types IIax (approximately 50% IIa and 50% IIx fibres) and IIb+ (60% IIb fibres, plus IIx and IIa). At rest, pure type I fibres displayed a much higher apparent Km for ADP (212 μm) than IIx fibres (8 μm). Within the IIax and IIb+ mixed fibre bundle types, two KADPm values were observed (70 μm and 5 μm). Comparison between pure IIx and mixed types indicates that the intermediate Km of 70 μm most probably corresponds to the mitochondrial affinity for ADP in IIa fibres, the lowest Km for ADP (5 μm) corresponding to IIx and IIb types. Activation of mitochondrial creatine and adenylate kinase reactions stimulated mitochondrial respiration only in type I and IIax fibre bundles, indicating an efficient coupling between both kinases and ADP rephosphorylation in type I and, likely, IIa fibres, since no effect was observed in pure IIx fibres. Following Ca<sup>2+</sup> -induced activation of myosin-ATPase, an increase in mitochondrial sensitivity to ADP of 45% and 250% was observed in type IIax and I bundles, respectively, an effect mostly prevented by addition of vanadate, an inhibitor of myosin-ATPase. Ca<sup>2+</sup> -induced activation of myosin-ATPase also prevented the stimulation of respiration rates by creatine and AMP in I and IIax bundles. In addition to differential regulation of mitochondrial respiration and energy transfer systems at rest in I and IIa versus IIx and IIb muscle fibres, our results indicate a regulation of phosphotransfer systems by Ca<sup>2+</sup> via the stimulation of myosin-ATPases in type I and IIa fibres of rabbit muscles.
|abstract=Mitochondrial respiration rates and their regulation by ADP, AMP and creatine, were studied at different free Ca<sup>2+</sup>  concentrations (0.1 versus 0.4 μm) on permeabilized fibre bundles of rabbit skeletal muscles differing in their myosin heavy chain profiles. Four fibre bundle types were obtained: pure types I and IIx, and mixed types IIax (approximately 50% IIa and 50% IIx fibres) and IIb+ (60% IIb fibres, plus IIx and IIa). At rest, pure type I fibres displayed a much higher apparent Km for ADP (212 μm) than IIx fibres (8 μm). Within the IIax and IIb+ mixed fibre bundle types, two KADPm values were observed (70 μm and 5 μm). Comparison between pure IIx and mixed types indicates that the intermediate Km of 70 μm most probably corresponds to the mitochondrial affinity for ADP in IIa fibres, the lowest Km for ADP (5 μm) corresponding to IIx and IIb types. Activation of mitochondrial creatine and adenylate kinase reactions stimulated mitochondrial respiration only in type I and IIax fibre bundles, indicating an efficient coupling between both kinases and ADP rephosphorylation in type I and, likely, IIa fibres, since no effect was observed in pure IIx fibres. Following Ca<sup>2+</sup> -induced activation of myosin-ATPase, an increase in mitochondrial sensitivity to ADP of 45% and 250% was observed in type IIax and I bundles, respectively, an effect mostly prevented by addition of vanadate, an inhibitor of myosin-ATPase. Ca<sup>2+</sup> -induced activation of myosin-ATPase also prevented the stimulation of respiration rates by creatine and AMP in I and IIax bundles. In addition to differential regulation of mitochondrial respiration and energy transfer systems at rest in I and IIa versus IIx and IIb muscle fibres, our results indicate a regulation of phosphotransfer systems by Ca<sup>2+</sup> via the stimulation of myosin-ATPases in type I and IIa fibres of rabbit muscles.
|mipnetlab=FR_Saint Gilles_Lefaucheur L, FR_Angers_Douay O
|keywords=Rabbit
|discipline=Mitochondrial Physiology
|mipnetlab=FR Saint Gilles Lefaucheur L, FR Angers Gueguen N
}}
}}
== Cited by ==
{{Template:Cited by Gnaiger 2020 BEC MitoPathways}}
{{Labeling
{{Labeling
|instruments=Oxygraph-2k
|organism=Rabbit
|organism=Other Mammal
|tissues=Skeletal muscle
|tissues=Skeletal muscle
|preparations=Permeabilized tissue, Enzyme
|preparations=Permeabilized tissue, Enzyme
|topics=Respiration; OXPHOS; ETS Capacity, Substrate; Glucose; TCA Cycle
|topics=Substrate
|discipline=Mitochondrial Physiology
|couplingstates=OXPHOS
|instruments=Oxygraph-2k
|additional=BEC 2020.2
}}
}}

Latest revision as of 16:13, 16 January 2021

Publications in the MiPMap
Gueguen N, Lefaucheur L, Ecolan P, Fillaut M, Herpin P (2005) Ca2+-activated myosin-ATPases, creatine and adenylate kinases regulate mitochondrial function according to myofibre type in rabbit. J Physiol 564:723-35.

» PMID: 15731190 Open Access

Gueguen N, Lefaucheur L, Ecolan P, Fillaut M, Herpin P (2005) J Physiol

Abstract: Mitochondrial respiration rates and their regulation by ADP, AMP and creatine, were studied at different free Ca2+ concentrations (0.1 versus 0.4 μm) on permeabilized fibre bundles of rabbit skeletal muscles differing in their myosin heavy chain profiles. Four fibre bundle types were obtained: pure types I and IIx, and mixed types IIax (approximately 50% IIa and 50% IIx fibres) and IIb+ (60% IIb fibres, plus IIx and IIa). At rest, pure type I fibres displayed a much higher apparent Km for ADP (212 μm) than IIx fibres (8 μm). Within the IIax and IIb+ mixed fibre bundle types, two KADPm values were observed (70 μm and 5 μm). Comparison between pure IIx and mixed types indicates that the intermediate Km of 70 μm most probably corresponds to the mitochondrial affinity for ADP in IIa fibres, the lowest Km for ADP (5 μm) corresponding to IIx and IIb types. Activation of mitochondrial creatine and adenylate kinase reactions stimulated mitochondrial respiration only in type I and IIax fibre bundles, indicating an efficient coupling between both kinases and ADP rephosphorylation in type I and, likely, IIa fibres, since no effect was observed in pure IIx fibres. Following Ca2+ -induced activation of myosin-ATPase, an increase in mitochondrial sensitivity to ADP of 45% and 250% was observed in type IIax and I bundles, respectively, an effect mostly prevented by addition of vanadate, an inhibitor of myosin-ATPase. Ca2+ -induced activation of myosin-ATPase also prevented the stimulation of respiration rates by creatine and AMP in I and IIax bundles. In addition to differential regulation of mitochondrial respiration and energy transfer systems at rest in I and IIa versus IIx and IIb muscle fibres, our results indicate a regulation of phosphotransfer systems by Ca2+ via the stimulation of myosin-ATPases in type I and IIa fibres of rabbit muscles. Keywords: Rabbit

O2k-Network Lab: FR Saint Gilles Lefaucheur L, FR Angers Gueguen N

Cited by

Gnaiger 2020 BEC MitoPathways
Gnaiger E (2020) Mitochondrial pathways and respiratory control. An introduction to OXPHOS analysis. 5th ed. Bioenerg Commun 2020.2. https://doi.org/10.26124/bec:2020-0002



Labels:


Organism: Rabbit  Tissue;cell: Skeletal muscle  Preparation: Permeabilized tissue, Enzyme 

Regulation: Substrate  Coupling state: OXPHOS 

HRR: Oxygraph-2k 

BEC 2020.2