Difference between revisions of "St-Pierre 2000 Proc Natl Acad Sci U S A"
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ATP use by the F1F0-ATPase might account for '9% of the ATP | ATP use by the F1F0-ATPase might account for '9% of the ATP | ||
turnover in anoxic frog skeletal muscle. | turnover in anoxic frog skeletal muscle. | ||
|mipnetlab=UK Cambridge Boutilier RG | |||
|discipline=Mitochondrial Physiology | |discipline=Mitochondrial Physiology | ||
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|organism=Other Non-Mammal | |organism=Other Non-Mammal | ||
|tissues=Skeletal muscle | |tissues=Skeletal muscle | ||
|preparations=Isolated Mitochondria | |||
|enzymes=Complex V; ATP Synthase | |enzymes=Complex V; ATP Synthase | ||
|kinetics=ADP; Pi, Oxygen | |kinetics=ADP; Pi, Oxygen | ||
|topics=Respiration; OXPHOS; ETS Capacity | |topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential | ||
|discipline=Mitochondrial Physiology | |discipline=Mitochondrial Physiology | ||
}} | }} | ||
Revision as of 04:18, 5 April 2012
| St-Pierre J, Brand MD, Boutilier RG (2000) Mitochondria as ATP consumers: Cellular treason in anoxia. Proc Natl Acad Sci USA 97: 8670-8674. |
St-Pierre J, Brand MD, Boutilier RG (2000) Proc Natl Acad Sci U S A
Abstract: In anoxia, mitochondria change from being ATP producers to potentially powerful ATP consumers. This change occurs, because the mitochondrial F1F0-ATPase begins to hydrolyze ATP to avoid the collapse of the proton motive force. Species that can survive prolonged periods of O2 lack must limit such ATP use; otherwise, this process would dominate glycolytic metabolism and threaten ATP delivery to essential ATP-consuming processes of the cell (e.g., ion-motive ATPases). There are two ways to limit ATP hydrolysis by the F1F0-ATPase, namely (i) reduction of the proton conductance of the mitochondrial inner membrane and (ii) inhibition of the enzyme. We assessed these two possibilities by using intact mitochondria isolated from the skeletal muscle of anoxia-tolerant frogs. Our results show that proton conductance is unaltered between normoxia and anoxia. However, ATP use by the F1F0-ATPase is limited in anoxia by a profound inhibition of the enzyme. Even so, ATP use by the F1F0-ATPase might account for '9% of the ATP turnover in anoxic frog skeletal muscle.
• O2k-Network Lab: UK Cambridge Boutilier RG
Labels:
Organism: Other Non-Mammal"Other Non-Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Tissue;cell: Skeletal muscle
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Enzyme: Complex V; ATP Synthase"Complex V; ATP Synthase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
Regulation: Respiration; OXPHOS; ETS Capacity"Respiration; OXPHOS; ETS Capacity" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property., Coupling; Membrane Potential"Coupling; Membrane Potential" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
HRR: Oxygraph-2k
