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  • Title: Isolation and partial characterization of a full-length cDNA clone for 3 alpha-hydroxysteroid dehydrogenase: a potential target enzyme for nonsteroidal anti-inflammatory drugs.
    Author: Pawlowski J, Huizinga M, Penning TM.
    Journal: Agents Actions; 1991 Sep; 34(1-2):289-93. PubMed ID: 1793046.
    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.
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