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Interaction of 125I-neuropeptide Y with rat cardiac membranes.

作者信息

Sheriff S, Rigel D F, Fischer J E, Balasubramaniam A

机构信息

Department of Surgery, University of Cincinnati Medical Center, Ohio 45267.

出版信息

Neuropeptides. 1990 Mar;15(3):157-60. doi: 10.1016/0143-4179(90)90148-r.

DOI:10.1016/0143-4179(90)90148-r
PMID:2174520
Abstract

125I-Neuropeptide Y (NPY) bound specifically with high affinity to rat atrial and ventricular membranes. Scatchard analysis revealed the presence of single class of binding sites in both atrial and ventricular membranes. The apparent Kd and Bmax for atrial membranes were 0.63 nM and 70 fmol/mg protein, respectively; ventricular membranes had an apparent kd of 0.39 nM and a Bmax of 283 fmol/mg protein. NPY structural homologues peptide YY (PYY) and pancreatic polypeptide (PP) bound to the ventricular membranes NPY receptor, but with several fold lower potency compared to NPY. Binding of 125I-NPY to ventricular membranes was sensitive to guanosine triphosphate (GTP) suggesting that the NPY receptor is linked to adenylate cyclase system. The receptor characterized in this system may play a crucial role in mediating the cardiac effects of NPY.

摘要

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