A physico-chemical comparison of aortic receptors in rat hypertension models

Walter J. Meyer; Nancy R. Nichols; Hanh H. Nguyen

doi:10.1016/0024-3205(86)90183-9

A physico-chemical comparison of aortic receptors in rat hypertension models

Walter J. Meyer
, Nancy R. Nichols
, Hanh H. Nguyen

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

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 cortocoid 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.

Original language	English (US)
Pages (from-to)	1231-1236
Number of pages	6
Journal	Life Sciences
Volume	39
Issue number	14
DOIs	https://doi.org/10.1016/0024-3205(86)90183-9
State	Published - Oct 6 1986
Externally published	Yes

ASJC Scopus subject areas

General Pharmacology, Toxicology and Pharmaceutics
General Biochemistry, Genetics and Molecular Biology

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10.1016/0024-3205(86)90183-9

Cite this

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title = "A physico-chemical comparison of aortic receptors in rat hypertension models",

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 cortocoid 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.",

author = "Meyer, \{Walter J.\} and Nichols, \{Nancy R.\} and Nguyen, \{Hanh H.\}",

note = "Funding Information: This work was supported by the NIH Research Grant NS 07189 and HI 20201. thank Ms. Gloria Collins for typing this manuscript. Funding Information: The void volume peak of protein-bound radioactivity (approx. 5ml) was manually applied to the top of the DE-52 resin bed with a Pasteur pipette. Subsequently, the column was washed with 60-70 ml of the starting buffer (pre-wash) and 4 ml fractions were collected. The protein was eluted with a 120 ml linear gradient of 1 mM-200 mM Na-phosphate (pH 7.5) in 20\% glycerol containing 1 mM EDTA at a flow rate of 35 ml/h (fraction volumne = 2 ml). Recoveries were based on the radioactivity (dpm) of the applied sample (G-25 void volume peak of protein-bound steroid) and were 65-70\% for whole cell receptor preparations. Conductivity was measured with a Chemtrix Type 70 conductivity meter. Protein was deteced by absorbance at 280 nm in a Zeiss PMQII spectrophotomet\textasciitilde{}r. Elution profiles were graphed using the CLINFO Data Management and Analysis System (supported by the Clinical Research Center Program Grant No. RR73, The University of Texas Medical Branch, Galveston).",

year = "1986",

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doi = "10.1016/0024-3205(86)90183-9",

language = "English (US)",

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pages = "1231--1236",

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T1 - A physico-chemical comparison of aortic receptors in rat hypertension models

AU - Meyer, Walter J.

AU - Nichols, Nancy R.

AU - Nguyen, Hanh H.

N1 - Funding Information: This work was supported by the NIH Research Grant NS 07189 and HI 20201. thank Ms. Gloria Collins for typing this manuscript. Funding Information: The void volume peak of protein-bound radioactivity (approx. 5ml) was manually applied to the top of the DE-52 resin bed with a Pasteur pipette. Subsequently, the column was washed with 60-70 ml of the starting buffer (pre-wash) and 4 ml fractions were collected. The protein was eluted with a 120 ml linear gradient of 1 mM-200 mM Na-phosphate (pH 7.5) in 20% glycerol containing 1 mM EDTA at a flow rate of 35 ml/h (fraction volumne = 2 ml). Recoveries were based on the radioactivity (dpm) of the applied sample (G-25 void volume peak of protein-bound steroid) and were 65-70% for whole cell receptor preparations. Conductivity was measured with a Chemtrix Type 70 conductivity meter. Protein was deteced by absorbance at 280 nm in a Zeiss PMQII spectrophotomet~r. Elution profiles were graphed using the CLINFO Data Management and Analysis System (supported by the Clinical Research Center Program Grant No. RR73, The University of Texas Medical Branch, Galveston).

PY - 1986/10/6

Y1 - 1986/10/6

N2 - 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 cortocoid 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.

AB - 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 cortocoid 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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ER -

A physico-chemical comparison of aortic receptors in rat hypertension models

Abstract

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