Inhibition of copper-zinc superoxide dismutase activity by selected environmental xenobiotics

被引：41

作者：

Lewandowski, Lukasz ^{[1
]}

Kepinska, Marta ^{[1
]}

Milnerowicz, Halina ^{[1
]}

机构：

[1] Wroclaw Med Univ, Fac Pharm, Dept Biomed & Environm Anal, Borowska 211, PL-50556 Wroclaw, Poland

来源：

ENVIRONMENTAL TOXICOLOGY AND PHARMACOLOGY | 2018年 / 58卷

关键词：

Copper-zinc superoxide dismutase; Enzyme activity; Inhibition; CU; ZN-SUPEROXIDE DISMUTASE; OXIDATIVE STRESS; SACCHAROMYCES-CEREVISIAE; HYDROGEN-PEROXIDE; NICKEL CARBONYL; BINDING-SITE; CANCER-CELLS; 3-DIMENSIONAL STRUCTURE; MOLECULAR-MECHANISM; ANGSTROM RESOLUTION;

D O I：

10.1016/j.etap.2017.12.022

中图分类号：

X [环境科学、安全科学];

学科分类号：

08 ; 0830 ;

摘要：

The function of Cu,Zn-SOD is to dismutate superoxide into hydrogen peroxide and oxygen. This task is fulfilled due to structural nuances of the enzyme. Many environmental xenobiotics have been proved to inhibit Cu,Zn-SOD. Those compounds could be found not only in industrial sewage, cigarettes and various chemical agents some of them are used as drugs, drug production substrates or are the product of drug biotransformation. Cu,Zn-SOD exposition to these compounds leads to inhibition due to: copper ion chelation, unfolding the structure of the enzyme, affecting residues vital for activity maintenance. This review covers a selection of Cu,Zn-SOD inhibitors, referring to in vivo and in vitro study.

引用

页码：105 / 113

页数：9

共 110 条

[1] The Structure of Human Extracellular Copper-Zinc Superoxide Dismutase at 1.7 Å Resolution: Insights into Heparin and Collagen Binding [J].

Antonyuk, Svetlana V. ;

Strange, Richard W. ;

Marklund, Stefan L. ;

Hasnain, S. Samar .

JOURNAL OF MOLECULAR BIOLOGY, 2009, 388 (02) :310-326

[2] ESTRADIOL METABOLISM BY COMPLEMENTARY DEOXYRIBONUCLEIC ACID-EXPRESSED HUMAN CYTOCHROME-P450S [J].

AOYAMA, T ;

KORZEKWA, K ;

NAGATA, K ;

GILLETTE, J ;

GELBOIN, HV ;

GONZALEZ, FJ .

ENDOCRINOLOGY, 1990, 126 (06) :3101-3106

[3] Solution structure of apo Cu,Zn superoxide dismutase: Role of metal ions in protein folding [J].

Banci, L ;

Bertini, I ;

Cramaro, F ;

Del Conte, R ;

Viezzoli, MS .

BIOCHEMISTRY, 2003, 42 (32) :9543-9553

[4] Structure and dynamics of copper-free SOD: The protein before binding copper [J].

Banci, L ;

Bertini, I ;

Cantini, F ;

D'Onofrio, M ;

Viezzoli, MS .

PROTEIN SCIENCE, 2002, 11 (10) :2479-2492

[5] Mechanisms underlying the protective effect of zinc and selenium against cadmium-induced oxidative stress in zebrafish Danio rerio [J].

Banni, Mohamed ;

Chouchene, Lina ;

Said, Khaled ;

Kerkeni, Abdelhamid ;

Messaoudi, Imed .

BIOMETALS, 2011, 24 (06) :981-992

[6] PHOSPHATE INHIBITION OF THE COPPER-CONTAINING AND ZINC-CONTAINING SUPEROXIDE-DISMUTASE - A REEXAMINATION [J].

BEYER, WF ;

WANG, Y ;

FRIDOVICH, I .

BIOCHEMISTRY, 1986, 25 (20) :6084-6088

[7] Superoxide Dismutases Are Involved in Candida albicans Biofilm Persistence against Miconazole [J].

Bink, Anna ;

Vandenbosch, Davy ;

Coenye, Tom ;

Nelis, Hans ;

Cammue, Bruno P. A. ;

Thevissen, Karin .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 2011, 55 (09) :4033-4037

[8] INHIBITION OF CIS-PLATINUM NEPHROTOXICITY BY DIETHYLDITHIOCARBAMATE RESCUE IN A RAT MODEL [J].

BORCH, RF ;

PLEASANTS, ME .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (12) :6611-6614

[9] ESSENTIAL ARGINYL RESIDUES IN CU,ZN SUPEROXIDE-DISMUTASE FROM SACCHAROMYCES CEREVISIAE [J].

BORDERS, CL ;

JOHANSEN, JT .

CARLSBERG RESEARCH COMMUNICATIONS, 1980, 45 (03) :185-194

[10] ESSENTIALITY OF THE ACTIVE-SITE ARGININE RESIDUE FOR THE NORMAL CATALYTIC ACTIVITY OF CU,ZN SUPEROXIDE-DISMUTASE [J].

BORDERS, CL ;

SAUNDERS, JE ;

BLECH, DM ;

FRIDOVICH, I .

BIOCHEMICAL JOURNAL, 1985, 230 (03) :771-776

← 1 2 3 4 5 6 7 8 9 10 →