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Glucocorticoid receptors in rat kidney cortical tubules enriched in proximal and distal segments

Glucocorticoid receptors in rat kidney cortical tubules enriched in proximal and distal segments Abstract Cytoplasmic and nuclear binding of 3Htriamcinolone acetonide was assessed in isolated rat kidney cortical tubules, enriched in distal (fraction A) or in proximal segments (fraction B). The concentration dependence of specific 3Htriamcinolone acetonide binding in cytoplasm was determined (range = 4.4 X 10(-10) to 2.1 X 10(-7) M) and analyzed by a least-squares curve-fitting method. A single, high-affinity binding class with a dissociation constant of 1 X 10(-8) M (25 degrees C) was obtained in both fractions A and B. Based on competition for the 3Htriamcinolone acetonide sites, the following sequence of affinities was obtained: triamcinolone acetonide = dexamethasone > progesterone = corticosterone > d-aldosterone > 17 beta-estradiol. These specificities imply that these sites are glucocorticoid receptors. Fraction B contained 1.6 times more cytosol sites for 3Htriamcinolone acetonide than fraction A (5.0 +/- 0.5 X 10(-13) vs. 3.0 +/- 0.5 X 10(-13) mol/mg protein). In the presence of a onefold excess of d-aldosterone specific cytoplasmic binding of 3Htriamcinolone acetonide was 1.4-fold greater in fraction B than in fraction A, and specific nuclear binding was 1.3-fold greater in fraction B than in fraction A (5.1 +/- 0.6 X 10(-13) vs 4.0 +/- 0.5 X 10(-13) mol/mg DNA). These results and the measured lengths of proximal and distal tubules yielded estimates of a higher proximal content (three- to sixfold) compared to distal content of glucocorticoid receptors. Copyright © 1981 the American Physiological Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Renal Physiology The American Physiological Society

Glucocorticoid receptors in rat kidney cortical tubules enriched in proximal and distal segments

Mishina, T.; Scholer, D. W.; Edelman, I. S.
AJP - Renal Physiology , Volume 240 (1): F38 – Jan 1, 1981
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Publisher
The American Physiological Society
Copyright
Copyright © 1981 the American Physiological Society
ISSN
0363-6127
eISSN
1522-1466
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Abstract

Abstract Cytoplasmic and nuclear binding of 3Htriamcinolone acetonide was assessed in isolated rat kidney cortical tubules, enriched in distal (fraction A) or in proximal segments (fraction B). The concentration dependence of specific 3Htriamcinolone acetonide binding in cytoplasm was determined (range = 4.4 X 10(-10) to 2.1 X 10(-7) M) and analyzed by a least-squares curve-fitting method. A single, high-affinity binding class with a dissociation constant of 1 X 10(-8) M (25 degrees C) was obtained in both fractions A and B. Based on competition for the 3Htriamcinolone acetonide sites, the following sequence of affinities was obtained: triamcinolone acetonide = dexamethasone > progesterone = corticosterone > d-aldosterone > 17 beta-estradiol. These specificities imply that these sites are glucocorticoid receptors. Fraction B contained 1.6 times more cytosol sites for 3Htriamcinolone acetonide than fraction A (5.0 +/- 0.5 X 10(-13) vs. 3.0 +/- 0.5 X 10(-13) mol/mg protein). In the presence of a onefold excess of d-aldosterone specific cytoplasmic binding of 3Htriamcinolone acetonide was 1.4-fold greater in fraction B than in fraction A, and specific nuclear binding was 1.3-fold greater in fraction B than in fraction A (5.1 +/- 0.6 X 10(-13) vs 4.0 +/- 0.5 X 10(-13) mol/mg DNA). These results and the measured lengths of proximal and distal tubules yielded estimates of a higher proximal content (three- to sixfold) compared to distal content of glucocorticoid receptors. Copyright © 1981 the American Physiological Society

Journal

AJP - Renal Physiology – The American Physiological Society

Published: Jan 1, 1981

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