Properties and tissue distribution of mouse monomeric carbonyl reductase

Shuhei Ishikura; Yutaka Yamamoto; Kazuya Matsuura; Jianjun Wei; M. E. Hodes; Akira Hara

doi:10.1248/bpb.21.879

Properties and tissue distribution of mouse monomeric carbonyl reductase

Shuhei Ishikura, Yutaka Yamamoto, Kazuya Matsuura, Jianjun Wei, M. E. Hodes, Akira Hara^*

^*Corresponding author for this work

Pathology

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

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-hydroxysteroid 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 reverse transcription- polymerase chain reaction analyses showed that the enzyme protein and its mRNA are expressed in various mouse tissues.

Original language	English (US)
Pages (from-to)	879-881
Number of pages	3
Journal	Biological and Pharmaceutical Bulletin
Volume	21
Issue number	8
DOIs	https://doi.org/10.1248/bpb.21.879
State	Published - 1998

Keywords

Carbonyl reductase
Short-chain dehydrogenase/reductase family
Tissue distribution
mRNA expression

ASJC Scopus subject areas

Pharmacology
Pharmaceutical Science

Access to Document

10.1248/bpb.21.879

Cite this

@article{db846e757b054df2bfad13bb6afcdd64,

title = "Properties and tissue distribution of mouse monomeric carbonyl reductase",

abstract = "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-hydroxysteroid 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 reverse transcription- polymerase chain reaction analyses showed that the enzyme protein and its mRNA are expressed in various mouse tissues.",

keywords = "Carbonyl reductase, Short-chain dehydrogenase/reductase family, Tissue distribution, mRNA expression",

author = "Shuhei Ishikura and Yutaka Yamamoto and Kazuya Matsuura and Jianjun Wei and Hodes, {M. E.} and Akira Hara",

year = "1998",

doi = "10.1248/bpb.21.879",

language = "English (US)",

volume = "21",

pages = "879--881",

journal = "Biological and Pharmaceutical Bulletin",

issn = "0918-6158",

publisher = "Pharmaceutical Society of Japan",

number = "8",

}

TY - JOUR

T1 - Properties and tissue distribution of mouse monomeric carbonyl reductase

AU - Ishikura, Shuhei

AU - Yamamoto, Yutaka

AU - Matsuura, Kazuya

AU - Wei, Jianjun

AU - Hodes, M. E.

AU - Hara, Akira

PY - 1998

Y1 - 1998

N2 - 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-hydroxysteroid 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 reverse transcription- polymerase chain reaction analyses showed that the enzyme protein and its mRNA are expressed in various mouse tissues.

AB - 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-hydroxysteroid 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 reverse transcription- polymerase chain reaction analyses showed that the enzyme protein and its mRNA are expressed in various mouse tissues.

KW - Carbonyl reductase

KW - Short-chain dehydrogenase/reductase family

KW - Tissue distribution

KW - mRNA expression

UR - http://www.scopus.com/inward/record.url?scp=0031753221&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031753221&partnerID=8YFLogxK

U2 - 10.1248/bpb.21.879

DO - 10.1248/bpb.21.879

M3 - Article

C2 - 9743262

AN - SCOPUS:0031753221

SN - 0918-6158

VL - 21

SP - 879

EP - 881

JO - Biological and Pharmaceutical Bulletin

JF - Biological and Pharmaceutical Bulletin

IS - 8

ER -

Properties and tissue distribution of mouse monomeric carbonyl reductase

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this