Glutathione conjugates and their synthetic derivatives as inhibitors of glutathione-dependent enzymes involved in cancer and drug resistance

被引:65
作者
Burg, D [1 ]
Mulder, GJ [1 ]
机构
[1] Leiden Univ, Leiden Amsterdam Ctr Drug Res, Div Toxicol, NL-2333 CC Leiden, Netherlands
关键词
GSH; GST; MRP; gamma GT; DNA-PK;
D O I
10.1081/DMR-120015695
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Alterations in levels of glutathione (GSH) and glutathione-dependent enzymes have been implicated in cancer and multidrug resistance of tumor cells. The activity of a number of these, the multidrug resistance-associated protein 1, glutathione S-transferase, DNA-dependent protein kinase, glyoxalase I, and gamma-glutamyl transpeptidase, can be inhibited by GSH-conjugates and synthetic analogs thereof. In this review we focus on the function of these enzymes and carriers in cancer and anti-cancer drug resistance, in relation to their inhibition by GSH-conjugate analogs.
引用
收藏
页码:821 / 863
页数:43
相关论文
共 290 条
[1]   Acivicin induces apoptosis independently of γ-glutamyltranspeptidase activity [J].
Aberkane, H ;
Frank, P ;
Galteau, MM ;
Wellman, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 285 (05) :1162-1167
[2]   THE GLUTATHIONE-BINDING SITE IN GLUTATHIONE S-TRANSFERASES - INVESTIGATION OF THE CYSTEINYL, GLYCYL AND GAMMA-GLUTAMYL DOMAINS [J].
ADANG, AEP ;
BRUSSEE, J ;
VANDERGEN, A ;
MULDER, GJ .
BIOCHEMICAL JOURNAL, 1990, 269 (01) :47-54
[3]   INHIBITION OF GLUTATHIONE-S-TRANSFERASE 3-3 BY GLUTATHIONE DERIVATIVES THAT BIND COVALENTLY TO THE ACTIVE-SITE [J].
ADANG, AEP ;
MOREE, WJ ;
BRUSSEE, J ;
MULDER, GJ ;
VANDERGEN, A .
BIOCHEMICAL JOURNAL, 1991, 278 :63-68
[4]  
ADANG AEP, 1991, J BIOL CHEM, V266, P830
[5]  
ADANG AEP, 1988, BIOCHEM J, V255, P721
[6]   Regulation of JNK signaling by GSTp [J].
Adler, V ;
Yin, ZM ;
Fuchs, SY ;
Benezra, M ;
Rosario, L ;
Tew, KD ;
Pincus, MR ;
Sardana, M ;
Henderson, CJ ;
Wolf, CR ;
Davis, RJ ;
Ronai, Z .
EMBO JOURNAL, 1999, 18 (05) :1321-1334
[7]  
Ali-Osman F, 1997, CLIN CANCER RES, V3, P2253
[8]   INHIBITION BY GLUTATHIONE DERIVATIVES OF BOVINE LIVER GLYOXALASE-II (HYDROXYACYLGLUTATHIONE HYDROLASE) AS A PROBE OF THE N- AND S-SITES FOR SUBSTRATE BINDING [J].
ALTIMARI, A ;
DOUGLAS, KT .
BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 870 (02) :219-225
[9]   Structure, catalytic mechanism, and evolution of the glutathione transferases [J].
Armstrong, RN .
CHEMICAL RESEARCH IN TOXICOLOGY, 1997, 10 (01) :2-18
[10]  
Arts HJG, 1999, CLIN CANCER RES, V5, P2798