<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Islam MS</submitter><funding>Kobayashi Foundation</funding><funding>The Smoking Research Foundation of Japan</funding><funding>The Grant of National Center for Child Health and Development</funding><funding>Japan Society for the Promotion of Science</funding><pagination>2876</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8532638</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>11(10)</volume><pubmed_abstract>17β-hydroxysteroid dehydrogenase type 3 (HSD17B3) converts androstenedione (A4) into testosterone (T), which regulates sex steroid production. Because various mutations of the HSD17B3 gene cause disorder of sex differentiation (DSD) in multiple mammalian species, it is very important to reveal the molecular characteristics of this gene in various species. Here, we revealed the open reading frame of the ovine HSD17B3 gene. Enzymatic activities of ovine HSD17B3 and HSD17B1 for converting A4 to T were detected using ovine androgen receptor-mediated transactivation in reporter assays. Although HSD17B3 also converted estrone to estradiol, this activity was much weaker than those of HSD17B1. Although ovine HSD17B3 has an amino acid sequence that is conserved compared with other mammalian species</pubmed_abstract><journal>Animals : an open access journal from MDPI</journal><pubmed_title>Analyses of Molecular Characteristics and Enzymatic Activities of Ovine HSD17B3.</pubmed_title><pmcid>PMC8532638</pmcid><funding_grant_id>19K09794</funding_grant_id><funding_grant_id>215</funding_grant_id><funding_grant_id>2020G006</funding_grant_id><funding_grant_id>2021-A1</funding_grant_id><funding_grant_id>181</funding_grant_id><funding_grant_id>19K07117</funding_grant_id><pubmed_authors>Kitano T</pubmed_authors><pubmed_authors>Suzuki N</pubmed_authors><pubmed_authors>Ida T</pubmed_authors><pubmed_authors>Islam MS</pubmed_authors><pubmed_authors>Uwada J</pubmed_authors><pubmed_authors>Yazawa T</pubmed_authors><pubmed_authors>Kikuya KI</pubmed_authors><pubmed_authors>Yaegashi K</pubmed_authors><pubmed_authors>Sato T</pubmed_authors><pubmed_authors>Hayashi J</pubmed_authors><pubmed_authors>Miyashiro Y</pubmed_authors><pubmed_authors>Umezawa A</pubmed_authors><pubmed_authors>Takahashi S</pubmed_authors><pubmed_authors>Watanabe H</pubmed_authors><pubmed_authors>Sekiguchi T</pubmed_authors><pubmed_authors>Khan RI</pubmed_authors><pubmed_authors>Imamichi Y</pubmed_authors><pubmed_authors>Muranishi Y</pubmed_authors><pubmed_authors>Hasegawa K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Analyses of Molecular Characteristics and Enzymatic Activities of Ovine HSD17B3.</name><description>17β-hydroxysteroid dehydrogenase type 3 (HSD17B3) converts androstenedione (A4) into testosterone (T), which regulates sex steroid production. Because various mutations of the HSD17B3 gene cause disorder of sex differentiation (DSD) in multiple mammalian species, it is very important to reveal the molecular characteristics of this gene in various species. Here, we revealed the open reading frame of the ovine HSD17B3 gene. Enzymatic activities of ovine HSD17B3 and HSD17B1 for converting A4 to T were detected using ovine androgen receptor-mediated transactivation in reporter assays. Although HSD17B3 also converted estrone to estradiol, this activity was much weaker than those of HSD17B1. Although ovine HSD17B3 has an amino acid sequence that is conserved compared with other mammalian species</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Sep</publication><modification>2026-05-04T03:08:47.492Z</modification><creation>2024-11-08T11:39:45.859Z</creation></dates><accession>S-EPMC8532638</accession><cross_references><pubmed>34679897</pubmed><doi>10.3390/ani11102876</doi></cross_references></HashMap>