Arylamine activating sulfotransferase in liver

作者：Nagata K; Yoshinari K; Ozawa S; Yamazoe Y

来源：Mutation Research-Fundamental and Molecular Mechanisms of Mutagenesis, 1997, 376(1-2): 267-272.

DOI：10.1016/S0027-5107(97)00052-3

• N-hydroxyaryl compound sulfation
• rat sulfotransferase
• human sulfotransferase
• N-hydroxy-2-acetylaminofluorene activation
• arylamine metabolism

Carcinogenic N-hydroxy-arylamines and -arylamides undergo metabolic activation by several enzymes in mammals to cause the DNA damage. Cytosolic sulfotransferases in rat and human livers, which belong to the ST1 (SULT1) family, have been studied to assess their properties to mediate the metabolic activation. A human orthologue of rat ST1C1 form, which catalyzes sulfation of N-hydroxy-2-acetylaminofluorene, was screened in a EMBL genomic library with ST1C1 cDNA [Nagata, K., S. Ozawa, M. Miyata, M. Shimada, D.-W. Gong, Y. Yamazoe and R. Kato (1993) J. Biol. Chem., 268, 24720-24725]. Sequencing of the hybridized clones indicate that at least 3'-terminal region of human ST1C1 orthologue contains sequence highly homologous to rat ST1C1 at both nucleotide and deduced amino acid levels. The experiments using anti-rat ST1C1 antibody and nucleotide probes for human ST1C1 showed no detectable band in Western blots and an mRNA-detecting method with polymerase chain reaction, respectively, in human liver samples.

• 出版日期1997-5-12