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AJP - Renal Physiology, Vol 260, Issue 5 764-F767, Copyright © 1991 by American Physiological Society
ARTICLES |
J. L. Yau, A. D. Van Haarst, M. P. Moisan, S. Fleming, C. R. Edwards and J. R. Seckl
Department of Medicine, University of Edinburgh, Western General Hospital, United Kingdom.
11 beta-Hydroxysteroid dehydrogenase (11 beta-OHSD) protects nonspecific renal mineralocorticoid receptors from exposure to circulating glucocorticoid in vivo by catalyzing the conversion of corticosterone to inactive 11-dehydrocorticosterone. Although 11 beta-OHSD bioactivity and aldosterone binding sites are found in distal tubular cells, mineralocorticoid receptor and 11 beta-OHSD immunoreactivities are not colocalized. However, there are several kidney isoforms of 11 beta-OHSD, not all of which may be immunoreactive, whereas only a single mRNA species has been described. Using in situ hybridization we found 11 beta-OHSD mRNA is highly expressed in all renal tubular epithelia in the rat. It is therefore likely that 11 beta-OHSD is colocalized with mineralocorticoid receptors in distal tubular cells.
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