The mitochondrial F1FO-ATPase revealed double-faced roles: its main role of producing ATP seems to counteract the ability to cause cell death. Indeed, under conditions of Ca+2 accumulation, the F1FO-ATPase triggers the so-called Mitochondrial Permeability Transition (MPT) a lethal cellular event. Accordingly, F1FO-ATPase dymers would generate similar Ca+2-dependent currents to MPT pore ones [1]. The F1FO-ATPase is more effectively inhibited by nitrite (NO2-) when activated by Ca2+ than by the natural cofactor Mg+2. In the presence of Ca+2 or Mg+2, NO2- uncompetitively inhibits the enzyme with respect to ATP substrate and inhibition extent depends on the cation. While NO2- inhibition is not prevented by ascorbate, ruling out any S-nitrosylation, it is enhanced by hydrogen peroxide (H2O2). The H2O2–driven production of nitrogen dioxide radical (•NO2) could cause post-translational modifications of tyrosine residues in the catalytic F1 sector. Since NO2-, especially provided by Mediterranean diets, acts as a vascular endocrine nitric oxide reservoir, it may protect against MPT events under ischemia/reperfusion conditions. 1. Antoniel M. et al. 2014. Int J Mol Sci 15:7513-36.

Modulation of mitochondrial Ca+2 and Mg+2 dependent F1FO-ATPase by nitrite

NESCI, SALVATORE;VENTRELLA, VITTORIA;TROMBETTI, FABIANA;PAGLIARANI, ALESSANDRA
2014

Abstract

The mitochondrial F1FO-ATPase revealed double-faced roles: its main role of producing ATP seems to counteract the ability to cause cell death. Indeed, under conditions of Ca+2 accumulation, the F1FO-ATPase triggers the so-called Mitochondrial Permeability Transition (MPT) a lethal cellular event. Accordingly, F1FO-ATPase dymers would generate similar Ca+2-dependent currents to MPT pore ones [1]. The F1FO-ATPase is more effectively inhibited by nitrite (NO2-) when activated by Ca2+ than by the natural cofactor Mg+2. In the presence of Ca+2 or Mg+2, NO2- uncompetitively inhibits the enzyme with respect to ATP substrate and inhibition extent depends on the cation. While NO2- inhibition is not prevented by ascorbate, ruling out any S-nitrosylation, it is enhanced by hydrogen peroxide (H2O2). The H2O2–driven production of nitrogen dioxide radical (•NO2) could cause post-translational modifications of tyrosine residues in the catalytic F1 sector. Since NO2-, especially provided by Mediterranean diets, acts as a vascular endocrine nitric oxide reservoir, it may protect against MPT events under ischemia/reperfusion conditions. 1. Antoniel M. et al. 2014. Int J Mol Sci 15:7513-36.
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Salvatore Nesci; Vittoria Ventrella; Fabiana Trombetti; Alessandra Pagliarani
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11585/350115
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