Expression of an Isoform of the Testis-Specific Estrogen Sulfotransferase in the Murine Placenta during the Late Gestational Period
| Autor: | Katsumi Tsukazaki, Kyoko Takehara, Yuriko Iwamori, Kaneyuki Kubushiro, Masao Iwamori, Shiro Nozawa |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Male
Gene isoform Sulfotransferase DNA Complementary medicine.drug_class Placenta Molecular Sequence Data Biophysics Uterus Gene Expression Gestational Age Biology Transfection Biochemistry Isozyme Mice Pregnancy Testis medicine Animals Estrogen Sulfotransferase Cloning Molecular Molecular Biology chemistry.chemical_classification Mice Hairless Mice Inbred BALB C Base Sequence Sequence Homology Amino Acid Reverse Transcriptase Polymerase Chain Reaction Molecular biology Amino acid Enzyme Activation Isoenzymes medicine.anatomical_structure chemistry Organ Specificity Estrogen COS Cells Female Sulfotransferases |
| Zdroj: | Archives of Biochemistry and Biophysics. 394:201-208 |
| ISSN: | 0003-9861 |
| DOI: | 10.1006/abbi.2001.2545 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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