Sulfotransferase catalyzing sulfation of heterocyclic amines

Y. Yamazoe; K. Nagata; K. Yoshinari; K. Fujita; T. Shiraga; K. Iwasaki

doi:10.1016/S0304-3835(99)00136-6

Sulfotransferase catalyzing sulfation of heterocyclic amines

Y. Yamazoe, K. Nagata, K. Yoshinari, K. Fujita, T. Shiraga, K. Iwasaki

PHA - Life and Pharmaceutical Science

Research output: Contribution to journal › Article › peer-review

24 Citations (Scopus)

Abstract

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. Copyright (C) 1999 Elsevier Science Ireland Ltd.

Original language	English
Pages (from-to)	103-107
Number of pages	5
Journal	Cancer Letters
Volume	143
Issue number	2
DOIs	https://doi.org/10.1016/S0304-3835(99)00136-6
Publication status	Published - 1999 Sept 1

Keywords

Detoxication
Metabolic activation
N-Hydroxyarylamine O-sulfation
N-Sulfation
Sulfotransferase gene family

ASJC Scopus subject areas

Oncology
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0304-3835(99)00136-6

Cite this

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title = "Sulfotransferase catalyzing sulfation of heterocyclic amines",

abstract = "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. Copyright (C) 1999 Elsevier Science Ireland Ltd.",

keywords = "Detoxication, Metabolic activation, N-Hydroxyarylamine O-sulfation, N-Sulfation, Sulfotransferase gene family",

author = "Y. Yamazoe and K. Nagata and K. Yoshinari and K. Fujita and T. Shiraga and K. Iwasaki",

year = "1999",

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doi = "10.1016/S0304-3835(99)00136-6",

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volume = "143",

pages = "103--107",

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TY - JOUR

T1 - Sulfotransferase catalyzing sulfation of heterocyclic amines

AU - Yamazoe, Y.

AU - Nagata, K.

AU - Yoshinari, K.

AU - Fujita, K.

AU - Shiraga, T.

AU - Iwasaki, K.

PY - 1999/9/1

Y1 - 1999/9/1

N2 - 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. Copyright (C) 1999 Elsevier Science Ireland Ltd.

AB - 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. Copyright (C) 1999 Elsevier Science Ireland Ltd.

KW - Detoxication

KW - Metabolic activation

KW - N-Hydroxyarylamine O-sulfation

KW - N-Sulfation

KW - Sulfotransferase gene family

UR - http://www.scopus.com/inward/record.url?scp=0032783503&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032783503&partnerID=8YFLogxK

U2 - 10.1016/S0304-3835(99)00136-6

DO - 10.1016/S0304-3835(99)00136-6

M3 - Article

C2 - 10503886

AN - SCOPUS:0032783503

SN - 0304-3835

VL - 143

SP - 103

EP - 107

JO - Cancer Letters

JF - Cancer Letters

IS - 2

ER -

Sulfotransferase catalyzing sulfation of heterocyclic amines

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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