Sulfotransferase catalyzing sulfation of heterocyclic amines

被引：21

作者：

Yamazoe, Y ^{[1
]}

Nagata, K

Yoshinari, K

Fujita, K

Shiraga, T

Iwasaki, K

机构：

[1] Tohoku Univ, Fac Pharmaceut Sci, Div Drug Metab & Mol Toxicol, Aoba Ku, Sendai, Miyagi 9808578, Japan

[2] Fujisawa Pharmaceut Co Ltd, Pharmaceut & Pharmacokinet Res Labs, Dept Pharmacokinet & Drug Metab, Yodogawa Ku, Osaka 532, Japan

来源：

CANCER LETTERS | 1999年 / 143卷 / 02期

关键词：

N-sulfation; N-hydroxyarylamine O-sulfation; sulfotransferase gene family; metabolic activation; detoxication;

D O I：

10.1016/S0304-3835(99)00136-6

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Cytosolic sulfation of arylamines to form sulfamates is found to be mediated by sulfotransferases of three gene families (SULT1 to 3). Among them, a SULT3 form (ST3A1) showed a high selectivity for N-sulfation of N-substituted aryl and alicyclic compounds. SULT1 (phenol) and SULT2 (hydroxysteroid) sulfotransferases showed N-sulfating activities of carcinogenic heterocyclic amines. For N-hydroxyarylamine O-sulfation, SULT1 forms showed high activity. In rats, ST1C1 mediated the metabolic activation of N-hydroxyarylamines. However, the related form. (ST1C2) in humans showed the negligible activity. Instead, ST1A3 showed high metabolic activating abilities among human sulfotransferases. (C) 1999 Published by Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：103 / 107

页数：5

共 22 条

[1] SULFOTRANSFERASE-MEDIATED DNA-BINDING OF N-HYDROXYARYLAMINES(AMIDE) IN LIVER CYTOSOLS FROM HUMAN AND EXPERIMENTAL-ANIMALS [J].