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Salmon calcitonin binding and stimulation of cyclic AMP generation in rat skeletal muscle.

Abstract：

:Salmon calcitonin potently competes for amylin binding sites in rat brain and has amylin-like actions upon glucose metabolism in rat muscle. We report here that [125I]-salmon calcitonin binds to rat hindlimb muscle membranes with high affinity (Kd = 0.47 pM). Binding was inhibited by rat amylin (Ki = 2 nM), rat alpha CGRP (Ki = 8 nM), rat beta CGRP (Ki = 11 nM), and rat calcitonin (Ki = 64 nM). Binding was maximal when measured in a hypotonic NaHepes buffer, and was significantly reduced in affinity when salts of Mg++, Ca++, Na+ or K+ were present. Incubation of rat hindlimb muscle membranes with salmon calcitonin at concentrations of 10 pM and above stimulated cyclic AMP generation. These results describe a skeletal muscle binding site which may mediate some of the actions of exogenous salmon calcitonin and of endogenous amylin and related peptides upon skeletal muscle fuel metabolism.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kenney MA,Moore CX,Pittner R,Beaumont K

doi

10.1006/bbrc.1993.2433

subject

Has Abstract

pub_date

1993-11-30 00:00:00

pages

8-14

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)72433-2

journal_volume

197

pub_type

杂志文章

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