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Hydroxysteroid dehydrogenase

About: Hydroxysteroid dehydrogenase is a research topic. Over the lifetime, 1087 publications have been published within this topic receiving 28468 citations. The topic is also known as: hydroxysteroid dehydrogenase.


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Journal ArticleDOI
TL;DR: A method that easily evaluates enzymatic activity of 17β-HSD3 by quantifying the conversion from A4 to T using androgen receptor (AR)-mediated transactivation is adapted and applicable to detect the conversion of 11-ketoandrostenedione to 11- ketotestosterone by HSD17B3.

13 citations

Journal ArticleDOI
TL;DR: All 4 17BetaHSD isoforms are variably expressed in human anterior pituitary adenomas, which also show 17betaHSD enzyme activity, suggesting that 17 betaHSD may play an important role in regulating the local cellular levels of estradiol.
Abstract: 17Beta-hydroxysteroid dehydrogenase (17betaHSD) isoforms reversibly catalyze the final step in the formation of estradiol (E2) from estrone (E1) and the formation of testosterone from androstenedione. We have investigated 17betaHSD type 1, 2, 3, and 4 gene expression and 17betaHSD estrogenic activity in human anterior pituitary adenomas. 17BetaHSD messenger ribonucleic acid (mRNA) expression was studied by RT-PCR in 42 pituitary tumors and 3 normal pituitaries, 17betaHSD activity was studied in 11 tumors and 17betaHSD type 1 was immunolocalized in vitro in 6 tumors. 17BetaHSD type 1 gene expression was detected in 34 of 42 adenomas in all tumor subtypes; 17betaHSD type 2 mRNA was detected in 18 of 42 adenomas, but not in prolactinomas; 17betaHSD type 3 mRNA was detected in 12 of 42 adenomas, but not in corticotropinomas; 17betaHSD type 4 was expressed in 20 of 42 adenomas by all adenoma subtypes. Reversible 17betaHSD activity was found in 9 of 11 adenomas, and 17betaHSD type 1 immunopositivity was cytoplasmically distributed in all 6 adenomas in vitro. All 4 17betaHSD isoforms are variably expressed in human anterior pituitary adenomas, which also show 17betaHSD enzyme activity, suggesting that 17betaHSD may play an important role in regulating the local cellular levels of estradiol.

13 citations

Journal ArticleDOI
10 Jul 2002-Gene
TL;DR: Cloning a cDNA that encodes a novel short-chain dehydrogenase/reductase, SDR-O, conserved in mouse, human and rat is reported, suggesting that S DR-O may catalyse the metabolism of another class of nuclear receptor ligand and may regulate metabolism by binding substrates/products and/or by serving as a regulatory factor.

13 citations

Journal ArticleDOI
TL;DR: Findings support the role 3α-HSD in inflammation and suggest that hydroxysteroid dehydrogenases, hydroxyprostaglandin dehydrogenase and prostagland in F2α synthase may be members of a common gene family.
Abstract: Homogeneous 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD; EC 1.1.1.50) of rat liver cytosol is a monomeric (Mr 34000) NAD(P)+ dependent oxidoreductase which displays 9-, 11- & 15-hydroxyprostaglandin dehydrogenase activity. The enzyme is potently inhibited by nonsteroidal anti-inflammatory drugs (NSAIDs), suggesting that 3 alpha-HSD may be a target enzyme for NSAIDs. A monospecific, polyclonal anti-sera raised against the purified enzyme was used to screen a lambda gt11 expression library and oligonucleotide probes complementary to the 5' and 3' ends of immunopositive clones were used to isolate a 2.1 kb full-length cDNA. Digestion of the full-length cDNA with Eco RI generated two fragments of 1.1 and 1.0 kb in length. Both fragments were subcloned into pGEM3 and partially sequenced. The 1.1 kb fragment contains the C-terminus of 3 alpha-HSD which was confirmed by an in-frame stop codon and comparison of the predicted amino acid sequence to peptide sequence obtained from two endo lys-C peptides of 3 alpha-HSD. The 1.0 kb fragment is 5' to the 1.1 kb fragment and is sufficient in length to contain the remainder of the entire open reading frame for 3 alpha-HSD. Dideoxysequencing reveals significant sequence homology with bovine lung prostaglandin PGF2 alpha synthase. These findings support the role 3 alpha-HSD in inflammation and suggest that hydroxysteroid dehydrogenases, hydroxyprostaglandin dehydrogenases and prostaglandin F2 alpha synthase may be members of a common gene family.

13 citations

Journal ArticleDOI
TL;DR: In this article, the effect of 5-Aza-2′-deoxycytidine (5-dAzaC) on the methylation status of HSD17B1 and its expression and conversion of E1 to E2 in HGC-27 and EPG 85-257 GC cells was investigated.

13 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202319
202217
20218
202016
201916
20186