Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure

Academic Article


  • We have previously characterized the first human NAD+-dependent short chain dehydrogenase capable of oxidizing all-trans-retinol and androgens, and found only in the liver and skin. In a search for related human enzymes, we identified a partial open reading frame, which exhibited > 60% sequence identity to human RoDH-4. The full-length cDNA for this enzyme was determined in our laboratory by 5′-RACE PCR and was found to be identical to the recently reported novel type of oxidative human 3α-hydroxysteroid dehydrogenase (3α-HSD). Analysis of the genomic structure revealed that the gene for RoDH-like 3α-HSD has four translated exons and, possibly, a fifth exon that codes for the 5′-untranslated region. The gene for RoDH-4 appears to have only four exons. The positions of exon-intron boundaries and the sizes of the protein coding regions are identical in 3α-HSD and RoDH-4. Moreover, both genes are mapped to chromosome 12q13, and are located in a close proximity to each other. Both genes appear to have satellite pseudogenes. Thus, RoDH-4 and 3α-HSD genes share similar structural organization and cluster on human chromosome 12, near the gene for 11-cis retinol dehydrogenase. © 2001 Elsevier Science Ireland Ltd.
  • Published In

    Digital Object Identifier (doi)

    Author List

  • Kedishvili NY; Belyaeva OV; Gough WH
  • Start Page

  • 457
  • End Page

  • 467
  • Volume

  • 130-132