Molecular cloning, expression and characterization of a phenol sulfotransferase cDNA from mouse intestine

Hiroomi Tamura, Atsushi Miyawaki, Hiroyuki Yoneshima, Katsuhiko Mikoshiba, Michio Matsui

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

A sulfotransferase (ST) cDNA was isolated from a mouse intestinal cDNA library using a probe which was generated by reverse transcription (RT)-PCR based on the conserved amino acid sequences of the ST molecules. The isolated cDNA (1.1 kb) contained an 858 bp open reading frame encoding a 286 amino acid polypeptide with molecular weight of 33439. The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively. RT-PCR analyses showed abundant expression of the P-ST mRNA in the intestine as well as in the liver in the mouse tissues examined (brain, heart, intestine, kidney, liver and lung) of both sexes. E. coli-expressed enzyme is capable of catalyzing the sulfation of 2-naphthol at K(m)=3.3 μM and V(max)=3.33 nmol/min/mg protein and also showed sulfation activity for L-3,4-dihydroxyphenylalanine (L-DOPA) and dopamine. Among food constituents tested, tannic acid and epigallocatechin gallate strongly inhibited the P-ST activity in vitro.

Original languageEnglish
Pages (from-to)234-239
Number of pages6
JournalBiological and Pharmaceutical Bulletin
Volume22
Issue number3
Publication statusPublished - 1999 Mar

Fingerprint

Arylsulfotransferase
Molecular Cloning
Intestines
Complementary DNA
Phenol
Sulfotransferases
Liver
Reverse Transcription
Amino Acid Sequence
Polymerase Chain Reaction
Tannins
Levodopa
Gene Library
Open Reading Frames
Isoenzymes
Dopamine
Molecular Weight
Alcohols
Escherichia coli
Kidney

Keywords

  • Inhibition
  • Intestine
  • Sulfotransferase

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology, Toxicology and Pharmaceutics(all)

Cite this

Molecular cloning, expression and characterization of a phenol sulfotransferase cDNA from mouse intestine. / Tamura, Hiroomi; Miyawaki, Atsushi; Yoneshima, Hiroyuki; Mikoshiba, Katsuhiko; Matsui, Michio.

In: Biological and Pharmaceutical Bulletin, Vol. 22, No. 3, 03.1999, p. 234-239.

Research output: Contribution to journalArticle

Tamura, Hiroomi ; Miyawaki, Atsushi ; Yoneshima, Hiroyuki ; Mikoshiba, Katsuhiko ; Matsui, Michio. / Molecular cloning, expression and characterization of a phenol sulfotransferase cDNA from mouse intestine. In: Biological and Pharmaceutical Bulletin. 1999 ; Vol. 22, No. 3. pp. 234-239.
@article{6be0fd5ebf4c4dc9a2a19efbda69162e,
title = "Molecular cloning, expression and characterization of a phenol sulfotransferase cDNA from mouse intestine",
abstract = "A sulfotransferase (ST) cDNA was isolated from a mouse intestinal cDNA library using a probe which was generated by reverse transcription (RT)-PCR based on the conserved amino acid sequences of the ST molecules. The isolated cDNA (1.1 kb) contained an 858 bp open reading frame encoding a 286 amino acid polypeptide with molecular weight of 33439. The deduced amino acid sequence shares 55.1{\%} and 40.2{\%} identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8{\%}) and ST1B2 (71.0{\%}), respectively. RT-PCR analyses showed abundant expression of the P-ST mRNA in the intestine as well as in the liver in the mouse tissues examined (brain, heart, intestine, kidney, liver and lung) of both sexes. E. coli-expressed enzyme is capable of catalyzing the sulfation of 2-naphthol at K(m)=3.3 μM and V(max)=3.33 nmol/min/mg protein and also showed sulfation activity for L-3,4-dihydroxyphenylalanine (L-DOPA) and dopamine. Among food constituents tested, tannic acid and epigallocatechin gallate strongly inhibited the P-ST activity in vitro.",
keywords = "Inhibition, Intestine, Sulfotransferase",
author = "Hiroomi Tamura and Atsushi Miyawaki and Hiroyuki Yoneshima and Katsuhiko Mikoshiba and Michio Matsui",
year = "1999",
month = "3",
language = "English",
volume = "22",
pages = "234--239",
journal = "Biological and Pharmaceutical Bulletin",
issn = "0918-6158",
publisher = "Pharmaceutical Society of Japan",
number = "3",

}

TY - JOUR

T1 - Molecular cloning, expression and characterization of a phenol sulfotransferase cDNA from mouse intestine

AU - Tamura, Hiroomi

AU - Miyawaki, Atsushi

AU - Yoneshima, Hiroyuki

AU - Mikoshiba, Katsuhiko

AU - Matsui, Michio

PY - 1999/3

Y1 - 1999/3

N2 - A sulfotransferase (ST) cDNA was isolated from a mouse intestinal cDNA library using a probe which was generated by reverse transcription (RT)-PCR based on the conserved amino acid sequences of the ST molecules. The isolated cDNA (1.1 kb) contained an 858 bp open reading frame encoding a 286 amino acid polypeptide with molecular weight of 33439. The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively. RT-PCR analyses showed abundant expression of the P-ST mRNA in the intestine as well as in the liver in the mouse tissues examined (brain, heart, intestine, kidney, liver and lung) of both sexes. E. coli-expressed enzyme is capable of catalyzing the sulfation of 2-naphthol at K(m)=3.3 μM and V(max)=3.33 nmol/min/mg protein and also showed sulfation activity for L-3,4-dihydroxyphenylalanine (L-DOPA) and dopamine. Among food constituents tested, tannic acid and epigallocatechin gallate strongly inhibited the P-ST activity in vitro.

AB - A sulfotransferase (ST) cDNA was isolated from a mouse intestinal cDNA library using a probe which was generated by reverse transcription (RT)-PCR based on the conserved amino acid sequences of the ST molecules. The isolated cDNA (1.1 kb) contained an 858 bp open reading frame encoding a 286 amino acid polypeptide with molecular weight of 33439. The deduced amino acid sequence shares 55.1% and 40.2% identity with mouse liver aryl/phenol (mSTp1) and alcohol (mSTa1 or mSTa2) STs, respectively, and it is highly similar to those of rat and human liver phenol ST (P-ST) isozymes, ST1B1 (87.8%) and ST1B2 (71.0%), respectively. RT-PCR analyses showed abundant expression of the P-ST mRNA in the intestine as well as in the liver in the mouse tissues examined (brain, heart, intestine, kidney, liver and lung) of both sexes. E. coli-expressed enzyme is capable of catalyzing the sulfation of 2-naphthol at K(m)=3.3 μM and V(max)=3.33 nmol/min/mg protein and also showed sulfation activity for L-3,4-dihydroxyphenylalanine (L-DOPA) and dopamine. Among food constituents tested, tannic acid and epigallocatechin gallate strongly inhibited the P-ST activity in vitro.

KW - Inhibition

KW - Intestine

KW - Sulfotransferase

UR - http://www.scopus.com/inward/record.url?scp=0032939203&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032939203&partnerID=8YFLogxK

M3 - Article

VL - 22

SP - 234

EP - 239

JO - Biological and Pharmaceutical Bulletin

JF - Biological and Pharmaceutical Bulletin

SN - 0918-6158

IS - 3

ER -