Expression of an isoform of the testis-specific estrogen sulfotransferase in the murine placenta during the late gestational period

K. Takehara, K. Kubushiro, Y. Iwamori, K. Tsukazaki, S. Nozawa, M. Iwamori

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Cytosolic sulfotransferases play essential roles in regulating the activities and transfer of steroids. To evaluate their biological significance in the murine uterus and placenta during the course of gestation, we determined their activities with several steroids as substrates. Activated estrogen sulfotransferase (EST) was found in the placenta and uterus during the late gestational period. Reverse-transcribed cDNA of murine placental EST (mpEST) was isolated from mouse placenta at 18 days of gestation and its expression in the tissue coincided with a change in its enzyme activity. The open-reading frame of mpEST encodes a protein composed of 296 amino acids with a predicted molecular mass of 35.5 kDa and was revealed to be an isoform of the murine testis-specific EST gene (99.7%). Also, the amino acid sequence of mpEST showed 49.6 and 77.9% homology with human placental and endometrial EST, respectively, showing that it corresponds to human endometrial EST. COS-7 cells transfected with mpEST exhibited sulfotransferase activity with the phenolic hydroxy groups of steroids and artificial substrates. The best acceptor substrate was estrogen.

Original languageEnglish
Pages (from-to)201-208
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume394
Issue number2
DOIs
Publication statusPublished - 2001 Oct 15

Fingerprint

Placenta
Testis
Protein Isoforms
Expressed Sequence Tags
Sulfotransferases
Steroids
Uterus
Substrates
Amino Acids
Pregnancy
COS Cells
Enzyme activity
Molecular mass
Open Reading Frames
Amino Acid Sequence
Estrogens
Complementary DNA
Genes
estrone sulfotransferase
Tissue

Keywords

  • Artificial substrate
  • COS-7 expression
  • Estrogen
  • Gestational period
  • Isozyme
  • Placenta
  • Steroid
  • Sulfotransferase
  • Uterus

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Expression of an isoform of the testis-specific estrogen sulfotransferase in the murine placenta during the late gestational period. / Takehara, K.; Kubushiro, K.; Iwamori, Y.; Tsukazaki, K.; Nozawa, S.; Iwamori, M.

In: Archives of Biochemistry and Biophysics, Vol. 394, No. 2, 15.10.2001, p. 201-208.

Research output: Contribution to journalArticle

Takehara, K. ; Kubushiro, K. ; Iwamori, Y. ; Tsukazaki, K. ; Nozawa, S. ; Iwamori, M. / Expression of an isoform of the testis-specific estrogen sulfotransferase in the murine placenta during the late gestational period. In: Archives of Biochemistry and Biophysics. 2001 ; Vol. 394, No. 2. pp. 201-208.
@article{16a56883a3ab473bb679982bff6ae6be,
title = "Expression of an isoform of the testis-specific estrogen sulfotransferase in the murine placenta during the late gestational period",
abstract = "Cytosolic sulfotransferases play essential roles in regulating the activities and transfer of steroids. To evaluate their biological significance in the murine uterus and placenta during the course of gestation, we determined their activities with several steroids as substrates. Activated estrogen sulfotransferase (EST) was found in the placenta and uterus during the late gestational period. Reverse-transcribed cDNA of murine placental EST (mpEST) was isolated from mouse placenta at 18 days of gestation and its expression in the tissue coincided with a change in its enzyme activity. The open-reading frame of mpEST encodes a protein composed of 296 amino acids with a predicted molecular mass of 35.5 kDa and was revealed to be an isoform of the murine testis-specific EST gene (99.7{\%}). Also, the amino acid sequence of mpEST showed 49.6 and 77.9{\%} homology with human placental and endometrial EST, respectively, showing that it corresponds to human endometrial EST. COS-7 cells transfected with mpEST exhibited sulfotransferase activity with the phenolic hydroxy groups of steroids and artificial substrates. The best acceptor substrate was estrogen.",
keywords = "Artificial substrate, COS-7 expression, Estrogen, Gestational period, Isozyme, Placenta, Steroid, Sulfotransferase, Uterus",
author = "K. Takehara and K. Kubushiro and Y. Iwamori and K. Tsukazaki and S. Nozawa and M. Iwamori",
year = "2001",
month = "10",
day = "15",
doi = "10.1006/abbi.2001.2545",
language = "English",
volume = "394",
pages = "201--208",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Expression of an isoform of the testis-specific estrogen sulfotransferase in the murine placenta during the late gestational period

AU - Takehara, K.

AU - Kubushiro, K.

AU - Iwamori, Y.

AU - Tsukazaki, K.

AU - Nozawa, S.

AU - Iwamori, M.

PY - 2001/10/15

Y1 - 2001/10/15

N2 - Cytosolic sulfotransferases play essential roles in regulating the activities and transfer of steroids. To evaluate their biological significance in the murine uterus and placenta during the course of gestation, we determined their activities with several steroids as substrates. Activated estrogen sulfotransferase (EST) was found in the placenta and uterus during the late gestational period. Reverse-transcribed cDNA of murine placental EST (mpEST) was isolated from mouse placenta at 18 days of gestation and its expression in the tissue coincided with a change in its enzyme activity. The open-reading frame of mpEST encodes a protein composed of 296 amino acids with a predicted molecular mass of 35.5 kDa and was revealed to be an isoform of the murine testis-specific EST gene (99.7%). Also, the amino acid sequence of mpEST showed 49.6 and 77.9% homology with human placental and endometrial EST, respectively, showing that it corresponds to human endometrial EST. COS-7 cells transfected with mpEST exhibited sulfotransferase activity with the phenolic hydroxy groups of steroids and artificial substrates. The best acceptor substrate was estrogen.

AB - Cytosolic sulfotransferases play essential roles in regulating the activities and transfer of steroids. To evaluate their biological significance in the murine uterus and placenta during the course of gestation, we determined their activities with several steroids as substrates. Activated estrogen sulfotransferase (EST) was found in the placenta and uterus during the late gestational period. Reverse-transcribed cDNA of murine placental EST (mpEST) was isolated from mouse placenta at 18 days of gestation and its expression in the tissue coincided with a change in its enzyme activity. The open-reading frame of mpEST encodes a protein composed of 296 amino acids with a predicted molecular mass of 35.5 kDa and was revealed to be an isoform of the murine testis-specific EST gene (99.7%). Also, the amino acid sequence of mpEST showed 49.6 and 77.9% homology with human placental and endometrial EST, respectively, showing that it corresponds to human endometrial EST. COS-7 cells transfected with mpEST exhibited sulfotransferase activity with the phenolic hydroxy groups of steroids and artificial substrates. The best acceptor substrate was estrogen.

KW - Artificial substrate

KW - COS-7 expression

KW - Estrogen

KW - Gestational period

KW - Isozyme

KW - Placenta

KW - Steroid

KW - Sulfotransferase

KW - Uterus

UR - http://www.scopus.com/inward/record.url?scp=0035887104&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035887104&partnerID=8YFLogxK

U2 - 10.1006/abbi.2001.2545

DO - 10.1006/abbi.2001.2545

M3 - Article

C2 - 11594734

AN - SCOPUS:0035887104

VL - 394

SP - 201

EP - 208

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -