Coenzyme Q-dependent functions of plasma membrane in the aging process

被引:8
作者
Navas, Placido
Villalba, Jose Manuel
Lenaz, Giorgio
机构
[1] Univ Pablo Olavide, Ctr Andaluz Biol Desarrollo, Seville 41013, Spain
[2] Univ Cordoba, Dept Biol Celular Fisiol & Immunol, Cordoba 14071, Spain
[3] Univ Bologna, Dep Biochim G Moruzzi, I-40126 Bologna, Italy
关键词
aging; coenzyme Q; oxidative stress; plasma membrane; redox system;
D O I
10.1007/s11357-005-1632-z
中图分类号
R592 [老年病学]; C [社会科学总论];
学科分类号
03 ; 0303 ; 100203 ;
摘要
Coenzyme Q ( Q) is reduced in plasma membrane and mitochondria by NAD(P)H-dependent reductases providing reducing equivalents to maintain both respiratory chain and antioxidant protection. Reactive oxygen species (ROS) are accumulated in the aging process originating mainly in mitochondria but also in other membranes, such as plasma membrane partially by the loss of electrons from the semiquinone. The reduction of Q by NAD(P)H-dependent reductases in plasma membrane is responsible for providing its antioxidant capacity, preventing both the lipid peroxidation chain and the activation of the ceramide-dependent apoptosis pathway. Both Q content and its reductases are decreased in plasma membrane of aging mammals. Calorie restriction, which extends mammal life span, increases the content of Q in the plasma membrane and also activates Q reductases in this membrane. Both lipid peroxidation and ceramide production are decreased in the plasma membrane in calorie-restricted animals. Plasma membrane is, then, an important cellular component to control the aging process through its concentration and redox state of Q.
引用
收藏
页码:139 / 146
页数:8
相关论文
共 93 条
[1]   Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1 [J].
Arnold, RS ;
Shi, J ;
Murad, E ;
Whalen, AM ;
Sun, CQ ;
Polavarapu, R ;
Parthasarathy, S ;
Petros, JA ;
Lambeth, JD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (10) :5550-5555
[2]   Ubiquinol regeneration by plasma membrane ubiquinone reductase [J].
Arroyo, A ;
Navarro, F ;
Navas, P ;
Villalba, JM .
PROTOPLASMA, 1998, 205 (1-4) :107-113
[3]   Characterization of VDAC1 as a plasma membrane NADH-oxidoreductase [J].
Baker, MA ;
Ly, JD ;
Lawen, A .
BIOFACTORS, 2004, 21 (1-4) :215-221
[4]   Aging in vertebrates, and the effect of caloric restriction: a mitochondrial free radical production-DNA damage mechanism? [J].
Barja, G .
BIOLOGICAL REVIEWS, 2004, 79 (02) :235-251
[5]   Plasma membrane ubiquinone controls ceramide production and prevents cell death induced by serum withdrawal [J].
Barroso, MP ;
GomezDiaz, C ;
Villalba, JM ;
Buron, MI ;
LopezLluch, G ;
Navas, P .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1997, 29 (03) :259-267
[6]   Antioxidant pyruvate inhibits cardiac formation of reactive oxygen species through changes in redox state [J].
Bassenge, E ;
Sommer, O ;
Schwemmer, M ;
Bünger, R .
AMERICAN JOURNAL OF PHYSIOLOGY-HEART AND CIRCULATORY PHYSIOLOGY, 2000, 279 (05) :H2431-H2438
[7]   Involvement of retinoid X receptor α in coenzyme Q metabolism [J].
Bentinger, M ;
Turunen, M ;
Zhang, XX ;
Wan, YJY ;
Dallner, G .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 326 (03) :795-803
[8]   The role of DT-diaphorase in the maintenance of the reduced antioxidant form of coenzyme Q in membrane systems [J].
Beyer, RE ;
SeguraAguilar, J ;
DiBernardo, S ;
Cavazzoni, M ;
Fato, R ;
Fiorentini, D ;
Galli, MC ;
Setti, M ;
Landi, L ;
Lenaz, G .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (06) :2528-2532
[9]   NOX5 NAD(P)H oxidase regulates growth and apoptosis in DU 145 prostate cancer cells [J].
Brar, SS ;
Corbin, Z ;
Kennedy, TP ;
Hemendinger, R ;
Thornton, L ;
Bommarius, B ;
Arnold, RS ;
Whorton, AR ;
Sturrock, AB ;
Huecksteadt, TP ;
Quinn, MT ;
Krenitsky, K ;
Ardie, KG ;
Lambeth, JD ;
Hoidal, JR .
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY, 2003, 285 (02) :C353-C369
[10]   STUDIES ON ACTIVE TRANSFER OF REDUCING EQUIVALENTS INTO MITOCHONDRIA VIA MALATE-ASPARTATE SHUTTLE [J].
BREMER, J ;
DAVIS, EJ .
BIOCHIMICA ET BIOPHYSICA ACTA, 1975, 376 (03) :387-397