Expression of an Isoform of the Testis-Specific Estrogen Sulfotransferase in the Murine Placenta during the Late Gestational Period

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 s...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 2001-10, Vol.394 (2), p.201-208
Main Authors: Takehara, Kyoko, Kubushiro, Kaneyuki, Iwamori, Yuriko, Tsukazaki, Katsumi, Nozawa, Shiro, Iwamori, Masao
Format: Article
Language:English
Subjects:
Animals
artificial substrate
Base Sequence
Cloning, Molecular
COS Cells
COS-7 expression
DNA, Complementary - isolation & purification
Enzyme Activation
estrogen
Female
Gene Expression
Gestational Age
gestational period
Isoenzymes - biosynthesis
Isoenzymes - genetics
isozyme
Male
Mice
Mice, Hairless
Mice, Inbred BALB C
Molecular Sequence Data
Organ Specificity
placenta
Placenta - enzymology
Pregnancy
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
steroid
sulfotransferase
Sulfotransferases - biosynthesis
Sulfotransferases - genetics
Testis - enzymology
Transfection
uterus
Uterus - enzymology
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Summary: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.
ISSN:0003-9861
1096-0384
DOI:10.1006/abbi.2001.2545