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
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.
引用
收藏
页码:197 / 202
页数:6
相关论文
共 32 条
  • [21] Identification of New Proteins and Potential Mitochondrial F1F0-ATPase Inhibitor Factor 1-Associated Mechanisms in Arabidopsis thaliana Using iTRAQ-Based Quantitative Proteomic Analysis
    Chen, Cuiting
    Meng, Yiqing
    Hu, Zhongyuan
    Yang, Jinghua
    Zhang, Mingfang
    PLANTS-BASEL, 2021, 10 (11):
  • [22] From the Ca2+-activated F1FO-ATPase to the mitochondrial permeability transition pore: an overview
    Nesci, Salvatore
    Trombetti, Fabiana
    Ventrella, Vittoria
    Pagliarani, Alessandra
    BIOCHIMIE, 2018, 152 : 85 - 93
  • [24] Mitochondrial Ca2+-activated F1FO-ATPase hydrolyzes ATP and promotes the permeability transition pore
    Algieri, Cristina
    Trombetti, Fabiana
    Pagliarani, Alessandra
    Ventrella, Vittoria
    Bernardini, Chiara
    Fabbri, Micaela
    Forni, Monica
    Nesci, Salvatore
    ANNALS OF THE NEW YORK ACADEMY OF SCIENCES, 2019, 1457 (01) : 142 - 157
  • [25] The Effects Of Prohibitin1 On The Content And Synthesis Activity Of F0f1-atpase And Mitochondrial Function In C2c12 Cells
    Fang, Wen
    Fong, Hong
    Ji, Li Li
    MEDICINE AND SCIENCE IN SPORTS AND EXERCISE, 2018, 50 (05): : 33 - 33
  • [26] INHIBITION OF MITOCHONDRIAL-F-1-ATPASE ACTIVITY BY AN ANTI-ALPHA SUBUNIT MONOCLONAL-ANTIBODY WHICH MODIFIES INTERACTIONS BETWEEN CATALYTIC AND REGULATORY SITES
    MORADIAMELI, M
    JULLIARD, JH
    GODINOT, C
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1989, 264 (03) : 1361 - 1367
  • [27] Interleukin-3 withdrawal induces an early increase in mitochondrial membrane potential unrelated to the Bcl-2 fammily -: Roles of intracellular pH, ADP transport, and F0F1-ATPase
    Khaled, AR
    Reynolds, DA
    Young, HA
    Thompson, CB
    Muegge, K
    Durum, SK
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (09) : 6453 - 6462
  • [28] New insight in a new entity: the mitochondrial permeability transition pore arises from the Ca2+-activated F1FO-ATPases
    Nesci, Salvatore
    SCIENCE BULLETIN, 2018, 63 (03) : 143 - 145
  • [29] INHIBITION OF MITOCHONDRIAL F1-ATPASE ACTIVITY BY BINDING OF (2-AZIDO-)ADP TO A SLOWLY EXCHANGEABLE NONCATALYTIC NUCLEOTIDE BINDING-SITE
    EDEL, CM
    HARTOG, AF
    BERDEN, JA
    BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1101 (03) : 329 - 338
  • [30] MG2+-INDUCED ADP-DEPENDENT INHIBITION OF THE ATPASE ACTIVITY OF BEEF-HEART MITOCHONDRIAL COUPLING FACTOR-F1
    MINKOV, IB
    FITIN, AF
    VASILYEVA, EA
    VINOGRADOV, AD
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1979, 89 (04) : 1300 - 1306