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Titolo:
Mitochondria as ATP consumers: Cellular treason in anoxia
Autore:
St-Pierre, J; Brand, MD; Boutilier, RG;
Indirizzi:
Univ Cambridge, Dept Zool, Cambridge CB2 3EJ, England Univ Cambridge Cambridge England CB2 3EJ ool, Cambridge CB2 3EJ, England Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England Univ Cambridge Cambridge England CB2 1QW hem, Cambridge CB2 1QW, England
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 15, volume: 97, anno: 2000,
pagine: 8670 - 8674
SICI:
0027-8424(20000718)97:15<8670:MAACCT>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
METABOLIC DEPRESSION; CHANNEL ARREST; RESPIRATION; MEMBRANE; INSITU; SUPPRESSION; MECHANISMS; INHIBITOR; GRADIENT; OXYGEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: St-Pierre, J Univ Cambridge, Dept Zool, Downing St, Cambridge CB2 3EJ, England Univ Cambridge Downing St Cambridge England CB2 3EJ England
Citazione:
J. St-Pierre et al., "Mitochondria as ATP consumers: Cellular treason in anoxia", P NAS US, 97(15), 2000, pp. 8670-8674

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 O-2 lack must limit such ATP use; otherwise. this process would dominate glycolytic metabolism and threaten ATP delivery to essential ATE-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 approximate to 9% of the ATP turnover in anoxic frog skeletal muscle.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 17:30:54