Bioenergetics and cell death

被引:86
作者
Kushnareva, Yulia [1 ]
Newmeyer, Donald D. [1 ]
机构
[1] La Jolla Inst Allergy & Immunol, La Jolla, CA 92037 USA
来源
MITOCHONDRIAL RESEARCH IN TRANSLATIONAL MEDICINE | 2010年 / 1201卷
关键词
bioenergetics; mitochondria; apoptosis; cell death; external pathway of NADH oxidation; MITOCHONDRIAL PERMEABILITY TRANSITION; CYTOCHROME-C RELEASE; MEMBRANE PERMEABILIZATION; CASPASE ACTIVATION; NEURONAL DEATH; OVARIAN-CANCER; EXTERNAL NADH; APOPTOSIS; CARDIOLIPIN; NECROSIS;
D O I
10.1111/j.1749-6632.2010.05633.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Mitochondrial bioenergetic function is a key to cell life and death. Cells need energy not only to support their vital functions but also to die gracefully. Execution of an apoptotic program includes energy-dependent steps, including kinase signaling, formation of the apoptosome, and effector caspase activation. Under conditions of bioenergetic collapse, cells are diverted toward necrotic demise. Mitochondrial outer membrane permeabilization (MOMP) is a decisive event in the execution of apoptosis. It is also causally linked to a decline in bioenergetic function via different mechanisms, not merely due to cytochrome c dispersion. MOMP-induced bioenergetic deficiency is usually irreversible and commits cells to die, even when caspases are inactive. Here, we discuss the mechanisms by which MOMP impacts bioenergetics in different cell death paradigms.
引用
收藏
页码:50 / 57
页数:8
相关论文
共 56 条
[1]   GLUTAMATE-INDUCED NEURONAL DEATH - A SUCCESSION OF NECROSIS OR APOPTOSIS DEPENDING ON MITOCHONDRIAL-FUNCTION [J].
ANKARCRONA, M ;
DYPBUKT, JM ;
BONFOCO, E ;
ZHIVOTOVSKY, B ;
ORRENIUS, S ;
LIPTON, SA ;
NICOTERA, P .
NEURON, 1995, 15 (04) :961-973
[2]   Membrane protein degradation by AAA proteases in mitochondria [J].
Arnold, I ;
Langer, T .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2002, 1592 (01) :89-96
[3]   Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death [J].
Baines, Christopher P. ;
Kaiser, Robert A. ;
Sheiko, Tatiana ;
Craigen, William J. ;
Molkentin, Jeffery D. .
NATURE CELL BIOLOGY, 2007, 9 (05) :550-U122
[4]   Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death [J].
Baines, CP ;
Kaiser, RA ;
Purcell, NH ;
Blair, NS ;
Osinska, H ;
Hambleton, MA ;
Brunskill, EW ;
Sayen, MR ;
Gottlieb, RA ;
Dorn, GW ;
Robbins, J ;
Molkentin, JD .
NATURE, 2005, 434 (7033) :658-662
[5]   Mitochondria and cell death - Mechanistic aspects and methodological issues [J].
Bernardi, P ;
Scorrano, L ;
Colonna, R ;
Petronilli, V ;
Di Lisa, F .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 264 (03) :687-701
[6]  
BERNARDI P, 1981, J BIOL CHEM, V256, P7187
[7]   Membrane potential generation coupled to oxidation of external NADH in liver mitochondria [J].
Bodrova, ME ;
Dedukhova, VI ;
Mokhova, EN ;
Skulachev, VP .
FEBS LETTERS, 1998, 435 (2-3) :269-274
[8]   GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspase activation [J].
Colell, Anna ;
Ricci, Jean-Ehrland ;
Tait, Stephen ;
Milasta, Sandra ;
Maurer, Ulrich ;
Bouchier-Hayes, Lisa ;
Fitzgerald, Patrick ;
Guio-Carrion, Ana ;
Waterhouse, Nigel J. ;
Li, Cindy Wei ;
Mari, Bernard ;
Barbry, Pascal ;
Newmeyer, Donald D. ;
Beere, Helen M. ;
Green, Douglas R. .
CELL, 2007, 129 (05) :983-997
[9]   Apoptosome inactivation rescues proneural and neural cells from neurodegeneration [J].
Cozzolino, M ;
Ferraro, E ;
Ferri, A ;
Rigamonti, D ;
Quondamatteo, F ;
Ding, H ;
Xu, ZS ;
Ferrari, F ;
Angelini, DF ;
Rotilio, G ;
Cattaneo, E ;
Carri, MT ;
Cecconi, F .
CELL DEATH AND DIFFERENTIATION, 2004, 11 (11) :1179-1191