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Type I (mineralocorticoid) receptors in the guinea pig

Type I (mineralocorticoid) receptors in the guinea pig in the guinea 3181, Australia KATHY MYLES AND JOHN W. FUNDER Baker Medical Research Institute, Melbourne, Myles, Kathy, and John W. Funder. I (mineralocorticoid) receptors in the guinea . Am. J. Physiol. 267 (Endocrinol. Metab. 30): E268-E272, 1994.-The affinity, capacity, and specificity of (mineralocorticoid receptors, MR) in the guinea are indistinguishable from similar values determined in parallel studies in the rat. In both epithelial (kidney, colon) and nonepithelial (hippocampus, heart) cytosol preparations, aldosterone binds with a dissociation constant at 4°C of l-2 nM in both species; for both guinea and rat the tissue concentrations of MR are an order of magnitude higher in hippocampus and colon than in kidney or heart. In both species, aldosterone and cortisol appear to have equivalent affinity for MR, and corticosterone appears to have two- to fourfold higher affinity. Given the wide variety of differences between the guinea and other species in other components of the pituitary-adrenal axis (superagonist adrenocorticotropic hormone, high circulating cortisol, low levels of transcortin, low-affinity glucocorticoid receptors) the unexpected finding of pristine in the guinea suggests powerful specificity-conferring mechanisms to allow aldosterone occupancy of MR in epithelia and the possibility of further definition of the roles of such in http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Endocrinology and Metabolism The American Physiological Society

Type I (mineralocorticoid) receptors in the guinea pig

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Publisher
The American Physiological Society
Copyright
Copyright © 1994 the American Physiological Society
ISSN
0193-1849
eISSN
1522-1555
Publisher site
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Abstract

in the guinea 3181, Australia KATHY MYLES AND JOHN W. FUNDER Baker Medical Research Institute, Melbourne, Myles, Kathy, and John W. Funder. I (mineralocorticoid) receptors in the guinea . Am. J. Physiol. 267 (Endocrinol. Metab. 30): E268-E272, 1994.-The affinity, capacity, and specificity of (mineralocorticoid receptors, MR) in the guinea are indistinguishable from similar values determined in parallel studies in the rat. In both epithelial (kidney, colon) and nonepithelial (hippocampus, heart) cytosol preparations, aldosterone binds with a dissociation constant at 4°C of l-2 nM in both species; for both guinea and rat the tissue concentrations of MR are an order of magnitude higher in hippocampus and colon than in kidney or heart. In both species, aldosterone and cortisol appear to have equivalent affinity for MR, and corticosterone appears to have two- to fourfold higher affinity. Given the wide variety of differences between the guinea and other species in other components of the pituitary-adrenal axis (superagonist adrenocorticotropic hormone, high circulating cortisol, low levels of transcortin, low-affinity glucocorticoid receptors) the unexpected finding of pristine in the guinea suggests powerful specificity-conferring mechanisms to allow aldosterone occupancy of MR in epithelia and the possibility of further definition of the roles of such in

Journal

AJP - Endocrinology and Metabolism – The American Physiological Society

Published: Aug 1, 1994

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