PMID: 9166119May 1, 1997Paper

Evidence for isoforms of 11 beta-hydroxysteroid dehydrogenase in the liver and kidney of the guinea pig

The Journal of Endocrinology
M QuinklerS Diederich

Abstract

In the human and in rodents like the rat and mouse, the liver enzyme 11 beta-hydroxysteroid dehydrogenase type I (11 beta-HSD-I) is a functional oxidoreductase preferring NADP+/NADPH as cosubstrate, while the renal isoenzyme (11 beta-HSD-II) prefers NAD+ as cosubstrate, and seems to be a pure oxidase and protects the tubular, mineralocorticoid (MC) receptor from occupancy by cortisol and corticosterone. We studied the enzyme kinetics of 11 beta-HSDs in kidney and liver microsomes of the guinea pig, a species whose zoological classification is still a matter of debate. With a fixed concentration of 10(-6) mol/l cortisol, liver and kidney microsomes preferred NAD+ to NADP+ (10(-3) mol/l) for the conversion to cortisone. Kidney microsomes converted cortisol to cortisone with K(m) values of 0.64 mumol/l and 9.8 mumol/l with NAD+ and NADP+ as cosubstrates respectively. The reduction of cortisone to cortisol was slow with kidney microsomes, but could be markedly enhanced by adding an NADH/NADPH regenerating system: with NADPH as preferred cosubstrate, the approximate K(m) was 7.2 mumol/l. This indicated the existence of both isoenzymes in the guinea pig kidney. Liver microsomes oxidized cortisol to cortisone with similar K(m) and Vma...Continue Reading

Citations

Jan 18, 2002·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Sandra KongIeva Stupans
Jul 1, 1999·Clinical and Experimental Pharmacology & Physiology·O AinsahB A Khalid
Dec 21, 2000·General and Comparative Endocrinology·S K WasserS L Monfort
Aug 1, 2013·Physiological Reviews·Karen ChapmanJonathan Seckl
Jan 21, 2004·Biochimica Et Biophysica Acta·L SchipperJ Fink-Gremmels

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