Abstract |
Rat models of genetic hypertension include spontaneous hypertension and resistance or sensitivity to mineralocorticoid and salt induced hypertension. Previously, altered aldosterone binding to corticoid receptor I was found in aortic smooth muscle cells cultured from Fischer 344 rats which are extremely resistant to steroid and salt induced hypertension. The corticoid receptor I of Fisher 344 rats had a lower affinity than that of salt sensitive Wistar-Kyoto controls, as well as spontaneously hypertensive rats and Sprague-Dawley rats. In the present study, we have used DEAE-cellulose ion exchange chromatography to compare the structure (charge properties) and steroid specificity of vascular corticoid receptor I and II sites in these same rat hypertension models. No variations in ion exchange properties of type I and II receptors were found. Together with the lower aldosterone affinity of corticoid receptor I sites in Fischer 344 rats these data suggest an altered binding domain which is not seen as a difference in charge density of the receptor protein by ion exchange chromatography.
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Authors | W J Meyer 3rd, N R Nichols, H H Nguyen |
Journal | Life sciences
(Life Sci)
Vol. 39
Issue 14
Pg. 1231-6
(Oct 06 1986)
ISSN: 0024-3205 [Print] Netherlands |
PMID | 3762307
(Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Receptors, Glucocorticoid
- Aldosterone
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Topics |
- Aldosterone
(metabolism)
- Animals
- Aorta
(metabolism)
- Binding Sites
- Chromatography, DEAE-Cellulose
- Hypertension
(metabolism)
- Male
- Muscle, Smooth, Vascular
(metabolism)
- Rats
- Rats, Inbred F344
(metabolism)
- Rats, Inbred SHR
(metabolism)
- Rats, Inbred Strains
(metabolism)
- Rats, Inbred WKY
(metabolism)
- Receptors, Glucocorticoid
(metabolism)
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