Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
Volume 1802, Issue 1, Pages 221-227Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbadis.2009.08.008
Keywords
Mitochondria; Permeability transition; Adenine nucleotide translocase; FoF1-ATPase; ATP consumption
Funding
- Orszagos Tudomdnyos Kutatasi Alapprogram (OTKA)
- Magyar Tudomdnyos Akademia (MTA)
- Nemzeti Kutatasi es Technologiai Hivatal (NKTH)
- Egeszsegugyi Tudomdnyos Tanacs
- OTKA-NKTH [NF68294]
- OTKA [NNF78905]
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ATP provided by oxidative phosphorylation supports highly complex and energetically expensive cellular processes. Yet, in several pathological settings, mitochondria could revert to ATP consumption, aggravating an existing cellular pathology. Here we review (i) the pathological conditions leading to ATP hydrolysis by the reverse operation of the mitochondrial FoF1-ATPase, (ii) molecular and thermodynamic factors influencing the directionality of the FoF1-ATPase, (iii) the role of the adenine nucleotide translocase as the intermediary adenine nucleotide flux pathway between the cytosol and the mitochondrial matrix when mitochondria become ATP consumers, (iv) the role of the permeability transition pore in bypassing the ANT, thereby allowing the flux of ATP directly to the hydrolyzing FoF1-ATPase, (v) the impact of the permeability transition pore on glycolytic ATP production, and (vi) endogenous and exogenous interventions for limiting ATP hydrolysis by the mitochondrial FoF1-ATPase. (C) 2009 Elsevier B.V. All rights reserved.
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