Cloning of a cDNA for liver microsomal retinol dehydrogenase. A tissue-specific, short-chain alcohol dehydrogenase.

摘要: Abstract Retinoic acid, a hormone biosynthesized from retinol, controls numerous biological systems by regulating eukaryotic gene expression conception through death. This work reports the cloning and of liver cDNA encoding microsomal retinol dehydrogenase (RoDH), which catalyzes primary rate-limiting step in retinoic acid synthesis. The predicted amino sequence biochemical data obtained recombinant enzyme verify it as short-chain alcohol dehydrogenase. Like RoDH, recognized substrate bound to cellular retinol-binding protein, had higher activity with NADP rather than NAD, was stimulated ethanol or phosphatidylcholine, not inhibited 4-methylpyrazole, phenylarsine oxide carbenoxolone localized microsomes. RoDH physiological form holocellular K 0.9 μM, value lower 5 μM concentration binding protein liver. Northern Western blot analyses revealed only rat liver, despite enzymatic brain, kidney, lung, testes. These suggest that tissue-specific isozyme(s) short chain dehydrogenases catalyze first biogenesis further strengthen evidence “cassette” serves substrate.