Properties and Tissue Distribution of Mouse Monomeric Carbonyl Reductase

• Published in: Biological & pharmaceutical bulletin Vol. 21; no. 8; pp. 879 - 881
• Main Authors: ISHIKURA, Shuhei, YAMAMOTO, Yutaka, MATSUURA, Kazuya, WEI, Jianjun, HODES, M.E., HARA, Akira
• Format: Journal Article
• Language: English
• Published: Tokyo The Pharmaceutical Society of Japan 01.08.1998; Maruzen; Japan Science and Technology Agency
• Subjects: Alcohol Oxidoreductases - genetics; Alcohol Oxidoreductases - metabolism; Animals; Biological and medical sciences; carbonyl reductase; Cerebellum - enzymology; Fundamental and applied biological sciences. Psychology; Gene expression; Humans; Kinetics; Mice; Molecular and cellular biology; Molecular genetics; mRNA expression; RNA, Messenger - analysis; short-chain dehydrogenase/reductase family; Tissue Distribution; Cerebellum; Human; Enzyme; Rodentia; Central nervous system; Carbonyl reductase (NADPH); Reverse transcription; Gene expression; Polymerase chain reaction; Substrate; Tissue; Vertebrata; Mammalia; Messenger RNA; Mouse; Distribution; Immunoblotting assay; Oxidoreductases; Recombinant protein; Comparative study
• ISSN: 0918-6158; 1347-5215
• DOI: 10.1248/bpb.21.879

We previously cloned a cDNA for mouse cerebellum carbonyl reductase which shows more than 81% homology to the cDNAs for monomeric carbonyl reductases of the rat, rabbit and human, and for pig 20β-hydroxy-steroid dehydrogenase. In the present study, we expressed the recombinant monomeric enzyme (34 kDa and pI 8.3) from the cDNA and compared its properties with the recombinant human enzyme. The mouse and human enzymes showed similar functional properties, although they differed in kinetic constants for carbonyl substrates and in inhibitor sensitivity. Both enzymes lacked glutathione S-transferase activity. Western blot and reversetranscription-polymerase chain reaction analyses showed that the enzyme protein and its mRNA are expressed in various mouse tissues.