Back to Search
Start Over
Cloning of 17beta-hydroxysteroid dehydrogenase-I cDNAs from Japanese eel ovary.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2000 Dec 20; Vol. 279 (2), pp. 451-6. - Publication Year :
- 2000
-
Abstract
- 17beta-hydroxysteroid dehydrogenase-I (17beta-HSD-I) is a key steroidogenic enzyme for estradiol-17beta (E(2)) production. cDNAs encoding 17beta-HSD-I were cloned for the first time in lower vertebrates from the ovary of a teleost, the Japanese eel. The deduced amino acid sequence from these cDNAs was approximately 50% identical to mammalian 17beta-HSD-Is. 17beta-HSD-I mRNA was not detected in previtellogenic ovaries by Northern blotting. However, transcript abundance increased in early vitellogenic ovaries obtained from fish artificially matured by gonadotropic treatment, but thereafter did not appear to change further. Recombinant 17beta-HSD-I expressed in human kidney 293 cells selectively converted estrone to E(2), but androstenedione, testosterone, or E(2) were not converted to any other steroids. Although it is widely accepted that E(2) is produced from testosterone in other species of teleosts, the substrate specificity of eel 17beta-HSD-I suggests that a steroidogenic pathway for production of E(2) from androstenedione via estrone exists in the Japanese eel ovary.<br /> (Copyright 2000 Academic Press.)
- Subjects :
- 17-Hydroxysteroid Dehydrogenases chemistry
17-Hydroxysteroid Dehydrogenases metabolism
Amino Acid Sequence
Animals
Cell Line
Chickens
Cloning, Molecular
DNA, Complementary
Female
Humans
Japan
Male
Mammals
Molecular Sequence Data
Organ Specificity
RNA, Messenger genetics
Rats
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Substrate Specificity
Testis enzymology
Transcription, Genetic
Transfection
17-Hydroxysteroid Dehydrogenases genetics
Eels genetics
Ovary enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 279
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 11118307
- Full Text :
- https://doi.org/10.1006/bbrc.2000.3974