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Am J Physiol Endocrinol Metab 269: E253-E268, 1995;
0193-1849/95 $5.00
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AJP - Endocrinology and Metabolism, Vol 269, Issue 2 E253-E268, Copyright © 1995 by American Physiological Society

ARTICLES

Natriuretic peptide receptors in the fetal rat

J. Brown and Z. Zuo
Physiological Laboratory, Cambridge, United Kingdom.

In vitro autoradiography of rat fetuses from embryonic days 12-19 (E12-E19) showed widespread high-affinity specific binding sites for natriuretic peptides. The sites on E16 somites avidly bound C-type natriuretic peptide [CNP-(1-22)] as well as C-ANP, a synthetic ligand that selects the C-type natriuretic peptide receptor (NPR-C). Most somitic binding sites had high affinity for atrial natriuretic peptide [ANP-(1-28)], confirming their resemblance to NPR-C. A few had a lower apparent affinity for ANP-(1-28), suggesting that they might be NPR-B. CNP-(1-22) was more powerful than ANP-(1-28) as an agonist of guanosine 3',5'-cyclic monophosphate production in somites, and ATP augmented the action of CNP-(1-22). These observations further suggest the presence of NPR-B. However, with cross-linking of 3-[125I]iodo-0-tyrosyl rat CNP-(1-22) to somitic membranes followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, only a single 64-kDa binding protein was detected under reducing conditions. This is not consistent with intact approximately 120-kDa NPR-B. In vitro autoradiography of the binding of natriuretic peptides to E16 liver implied the presence of NPR-A and NPR-C-like receptors. Hepatic guanosine 3',5'-cyclic monophosphate production was most powerfully stimulated by ANP-(1-28), as expected for NPR-A. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis also identified NPR-A and NPR-C-like proteins in E16 hepatic membranes. Thus different NPRs are expressed by specific fetal tissues. This may be developmentally significant.


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