ArticleMolecular and cellular biochemistry2011
Identification and functional characterization of a putative 17β-hydroxysteroid dehydrogenase 12 in abalone (Haliotis diversicolor supertexta).
Article in Molecular and cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 19 citations in OpenAlex.
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The 17β-hydroxysteroid dehydrogenases (17β-HSDs) are key enzymes in the downstream process of steroid hormone biosynthesis. To date, relatively little is known about the role of 17β-HSDs in marine gastropods. In the present study, a putative cDNA sequence encoding type 12 17β-HSD (17β-HSD-12) was identified in abalone (Haliotis diversicolor supertexta). The full-length cDNA was 1,978 bp, including an open reading frame (ORF) of 963 bp that encoded a protein of 321 amino acids. Comparative structural analysis revealed that abalone 17β-HSD-12 shared 39.8-42.8% amino acid identity with other 17β-HSD-12 homologues and that the functional domains were well conserved. Phylogenetic analysis revealed that abalone 17β-HSD-12 belonged to the short-chain dehydrogenases/reductases (SDRs) family. Functional analysis following transient transfection of the ORF in human embryonic kidney-293 (HEK-293) cells indicated that abalone 17β-HSD-12 had the ability to convert estrone (E1) into estradiol (E2). Expression analysis in vivo demonstrated that abalone 17β-HSD-12 was differentially expressed during the three reproductive stages (pre-spawning, spawning, and post-spawning). These results indicate that abalone 17β-HSD-12 is an SDR family member with a key role in steroidogenesis during the reproductive period.
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