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AJP - Renal Physiology, Vol 257, Issue 3 414-F423, Copyright © 1989 by American Physiological Society
ARTICLES |
T. Huo and D. P. Healy
Department of Pharmacology, Mount Sinai School of Medicine, City University of New York, New York 10029.
Dopamine receptors in the rat kidney were characterized by homogenate binding and in vitro autoradiography using the dopamine 1 (DA1)-selective antagonist [3H]Sch 23390. [3H]Sch 23390 binding in cortical membrane preparations was saturable, stereoselective, and competed for by DA agonists and antagonists with a rank order of potency consistent with the labeling of the DA1 receptor. [3H]Sch 22390 binding was best fit to a two-site model: a high affinity-low density site (KD1 4.9 +/- 1.4 nM, Bmax 1 31.4 +/- 13.8 fmol/mg protein) and a low affinity-high density site (KD2 86.4 +/- 23.9 nM, Bmax 2 848.0 +/- 227.4 fmol/mg protein). In vitro autoradiography indicated that [3H]Sch 22390 binding sites were restricted to the cortex. High-resolution autoradiography further indicated that [3H]Sch 22390 binding sites were localized primarily on proximal tubules. Glomeruli and other vascular elements were devoid of [3H]Sch 23390 binding sites. These results suggest that DA and DA1 agonists may affect sodium excretion by a direct action on proximal tubule sodium reabsorption.
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