A physico-chemical comparison of aortic receptors in rat hypertension models |
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| Authors: | W J Meyer N R Nichols H H Nguyen |
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| Affiliation: | 1. The University of Texas Medical Branch Departments of Pediatrics, USA;2. Psychiatry & Behavioral Sciences, Galveston, Texas, 77550-2776, USA;1. Université Clermont Auvergne, Inserm U1107 Neuro-Dol, Pharmacologie Fondamentale et Clinique de la Douleur, Clermont-Ferrand, France;2. ANALGESIA Institute, Faculty of Medicine, 63000 Clermont-Ferrand, France;3. CiTCoM, CNRS - UMR 8038, INSERM U1268, Faculty of Pharmacy of Paris, University Paris Cité, 75270 Paris Cedex 06, France;4. Department of Pharmacy, Institut Curie, 75248 Paris Cedex 06, France;1. Internal Emergency Medicine Unit, Department of Medicine-DIMED University of Padua, Specialized Center for Blood Pressure Disorders-Regione Veneto, 35128 Padua, Italy;2. Department of Biomedical Sciences-DSB, University of Padua, 35131 Padua, Italy;3. Italian National Research Council (CNR), Neuroscience Institute, 35131 Padua, Italy |
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| 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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