Antioxidant enzymes and human diseases

被引:1561
作者
Matés, JM [1 ]
Pérez-Gómez, C [1 ]
De Castro, IN [1 ]
机构
[1] Univ Malaga, Fac Sci, Dept Mol Biol & Biochem, E-29071 Malaga, Spain
关键词
antioxidants; catalase; glutathione peroxidase; human diseases; oxidative damage; oxidative stress; reactive oxygen species; superoxide dismutase; therapy;
D O I
10.1016/S0009-9120(99)00075-2
中图分类号
R446 [实验室诊断]; R-33 [实验医学、医学实验];
学科分类号
1001 ;
摘要
Objectives: To describe the importance of the antioxidant enzymes superoxide dismutase, glutathione peroxidase, and catalase working together in human cells against toxic reactive oxygen species, their relationship with several pathophysiologic processes and their possible therapeutic implications. Conclusions: Reactive oxygen species (ROS) are involved in the cell growth, differentiation, progression, and death. Low concentrations of ROS may be beneficial or even indispensable in processes such as intracellular signaling and defense against micro-organisms. Nevertheless, higher amounts of ROS play a role in the aging process as well as in a number of human disease states, including cancer, ischemia, and failures in immunity and endocrine functions. As a safeguard against the accumulation of ROS, several nonenzymatic and enzymatic antioxidant activities exist. Therefore, when oxidative stress arises as a consequence of a pathologic event, a defense system promotes the regulation and expression of these enzymes. Copyright (C) 1999 The Canadian Society of Clinical Chemists.
引用
收藏
页码:595 / 603
页数:9
相关论文
共 136 条
[1]   Rheumatoid arthritis and metal compounds - perspectives on the role of oxygen radical detoxification [J].
Aaseth, J ;
Haugen, M ;
Forre, O .
ANALYST, 1998, 123 (01) :3-6
[2]  
Aebi HE, 1980, METHOD ENZYMAT AN, V3, P273
[3]   Oxidative damage, plasma antioxidant capacity, and glucemic control in elderly NIDDM patients [J].
Aguirre, F ;
Martin, I ;
Grinspon, D ;
Ruiz, M ;
Hager, A ;
De Paoli, T ;
Ihlo, J ;
Farach, HA ;
Poole, CP .
FREE RADICAL BIOLOGY AND MEDICINE, 1998, 24 (04) :580-585
[4]   Superoxide-mediated decomposition of biological S-nitrosothiols [J].
Aleryani, S ;
Milo, E ;
Rose, Y ;
Kostka, P .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (11) :6041-6045
[5]  
AMSTAD P, 1994, J BIOL CHEM, V269, P1606
[6]   Epidermal growth factor (EGF)-induced generation of hydrogen peroxide - Role in EGF receptor-mediated tyrosine phosphorylation [J].
Bae, YS ;
Kang, SW ;
Seo, MS ;
Baines, IC ;
Tekle, E ;
Chock, PB ;
Rhee, SG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (01) :217-221
[7]   The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration - Evidence for altered subunit interaction in all the bacteriocupreins [J].
Battistoni, A ;
Folcarelli, S ;
Gabbianelli, R ;
Capo, C ;
Rotilio, G .
BIOCHEMICAL JOURNAL, 1996, 320 :713-716
[8]   Role of the dimeric structure in Cu,Zn superoxide dismutase -: pH-dependent, reversible denaturation of the monomeric enzyme from Escherichia coli [J].
Battistoni, A ;
Folcarelli, S ;
Cervoni, L ;
Polizio, F ;
Desideri, A ;
Giartosio, A ;
Rotilio, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (10) :5655-5661
[9]   SELENIUM, GLUTATHIONE-PEROXIDASE AND ASTHMA [J].
BEASLEY, R ;
THOMSON, C ;
PEARCE, N .
CLINICAL AND EXPERIMENTAL ALLERGY, 1991, 21 (02) :157-159
[10]   Resistance of lipoprotein(a) to lipid peroxidation induced by oxygenated free radicals produced by gamma radiolysis: A comparison with low-density lipoprotein [J].
Beaudeux, JL ;
GardesAlbert, M ;
Delattre, J ;
Legrand, A ;
Rousselet, F ;
Peynet, J .
BIOCHEMICAL JOURNAL, 1996, 314 :277-284