The inhibition of the mitochondrial F1F0-ATPase activity when activated by Ca2+ opens new regulatory roles for NAD+

被引：4

作者：

Nesci, Salvatore ^{[1
]}

Trombetti, Fabiana ^{[1
]}

Ventrella, Vittoria ^{[1
]}

Pirini, Maurizio ^{[1
]}

Pagliarani, Alessandra ^{[1
]}

机构：

[1] Univ Bologna, Dept Vet Med Sci DIMEVET, Via Tolara Sopra 50, I-40064 Ozzano Dellemilia, BO, Italy

来源：

BIOLOGICAL CHEMISTRY | 2018年 / 399卷 / 02期

关键词：

Ca2+ cofactor; F1F0-ATPase; mitochondria; NAD(+); PERMEABILITY TRANSITION PORE; MUSSEL DIGESTIVE GLAND; MG-ATPASE ACTIVITY; SYNTHASE; SIRTUINS; F1FO-ATPASE; MECHANISM; DISEASE; NICOTINAMIDE; REPLACEMENT;

D O I：

10.1515/hsz-2017-0209

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The mitochondrial F1F0-ATPase is uncompetitively inhibited by NAD(+) only when the natural cofactor Mg2+ is replaced by Ca2+, a mode putatively involved in cell death. The Ca2+-dependent F1F0-ATPase is also inhibited when NAD(+) concentration in mitochondria is raised by acetoacetate. The enzyme inhibition by NAD(+) cannot be ascribed to any de-ac(et)ylation or ADP-ribosylation by sirtuines, as it is not reversed by nicotinamide. Moreover, the addition of acetyl-CoA or palmitate, which would favor the enzyme ac(et)ylation, does not affect the F1F0-ATPase activity. Consistently, NAD(+) may play a new role, not associated with redox and non-redox enzymatic reactions, in the Ca2+-dependent regulation of the F1F0-ATPase activity.

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收藏

页码：197 / 202

页数：6

相关论文

共 31 条

[1] Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase [J].

Allegretti, Matteo ;

Klusch, Niklas ;

Mills, Deryck J. ;

Vonck, Janet ;

Kuehlbrandt, Werner ;

Davies, Karen M. .

NATURE, 2015, 521 (7551) :237-+

[2] Stoichiometry of subunit e in rat liver mitochondrial H+-ATP synthase and membrane topology of its putative Ca2+-dependent regulatory region [J].

Arakaki, N ;

Ueyama, Y ;

Hirose, M ;

Himeda, T ;

Shibata, H ;

Futaki, S ;

Kitagawa, K ;

Higuti, T .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2001, 1504 (2-3) :220-228

[3] Mechanism of sirtuin inhibition by nicotinamide:: Altering the NAD+ cosubstrate specificity of a Sir2 enzyme [J].

Avalos, JL ;

Bever, KM ;

Wolberger, C .

MOLECULAR CELL, 2005, 17 (06) :855-868

[4] THE MITOCHONDRIAL PERMEABILITY TRANSITION PORE: CHANNEL FORMATION BY F-ATP SYNTHASE, INTEGRATION IN SIGNAL TRANSDUCTION, AND ROLE IN PATHOPHYSIOLOGY [J].

Bernardi, Paolo ;

Rasola, Andrea ;

Forte, Michael ;

Lippe, Giovanna .

PHYSIOLOGICAL REVIEWS, 2015, 95 (04) :1111-1155

[5] CaATP inhibition of the MgATP-dependent proton pump (H+-ATPase) in bacterial photosynthetic membranes with a mechanism of alternative substrate inhibition [J].

Casadio, R ;

Melandri, BA .

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 1996, 1 (04) :284-291

[6] Investigating the ADP-ribosyltransferage Activity of Sirtuins with NAD Analogues and 32P-NAD [J].

Du, Jintang ;

Jiang, Hong ;

Lin, Hening .

BIOCHEMISTRY, 2009, 48 (13) :2878-2890

[7] Sodium ion cycling mediates energy coupling between complex I and ATP synthase [J].

Gemperli, AC ;

Dimroth, P ;

Steuber, J .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (03) :839-844

[8] Ca2+ binding to F-ATP synthase β subunit triggers the mitochondrial permeability transition [J].

Giorgio, Valentina ;

Burchell, Victoria ;

Schiavone, Marco ;

Bassot, Claudio ;

Minervini, Giovanni ;

Petronilli, Valeria ;

Argenton, Francesco ;

Forte, Michael ;

Tosatto, Silvio ;

Lippe, Giovanna ;

Bernardi, Paolo .

EMBO REPORTS, 2017, 18 (07) :1065-1076

[9] Dimers of mitochondrial ATP synthase form the permeability transition pore [J].

Giorgio, Valentina ;

von Stockum, Sophia ;

Antoniel, Manuela ;

Fabbro, Astrid ;

Fogolari, Federico ;

Forte, Michael ;

Glick, Gary D. ;

Petronilli, Valeria ;

Zoratti, Mario ;

Szabo, Ildiko ;

Lippe, Giovanna ;

Bernardi, Paolo .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2013, 110 (15) :5887-5892

[10] Nicotinamide riboside restores cognition through an upregulation of proliferator-activated receptor-γ coactivator 1α regulated β-secretase 1 degradation and mitochondrial gene expression in Alzheimer's mouse models [J].

Gong, Bing ;

Pan, Yong ;

Vempati, Prashant ;

Zhao, Wei ;

Knable, Lindsay ;

Ho, Lap ;

Wang, Jun ;

Sastre, Magdalena ;

Ono, Kenjiro ;

Sauve, Anthony A. ;

Pasinetti, Giulio M. .

NEUROBIOLOGY OF AGING, 2013, 34 (06) :1581-1588

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