Characterization of specific binding of atrial natriuretic peptide (ANP) to rat PC12 phaeochromocytoma cells.
Specific binding sites for atrial natriuretic peptide have been identified in membrane of the phaeochromocytoma cell line PC12. Scatchard analysis of binding studies revealed a Kd of 794 pM and a density (Bmax) of 254 fmol/mg protein. Hormones unrelated to ANP such as angiotensin II, bradykinin and arginine-8-vasopressin did not complete for the binding sites. Of the ANP-related peptides which competed for the binding sites, the following order of affinity was established; rANP (8-33) greater than rANP (28 amino acid) greater than rat atrial peptide fragment (13-28) greater than a-hANP (28 amino acid) greater than atrial peptide fragment (1-11) greater than atriopeptin I.
Boumezrag
A
A
MRC Blood Pressure Unit, Western Infirmary, Glasgow, Scotland, U.K.
Lyall
F
F
Dow
J A
JA
D000310:Adrenal Gland Neoplasms / Q000378:metabolism; D000818:Animals; D009320:Atrial Natriuretic Factor / Q000378:metabolism*; D001667:Binding, Competitive; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D007700:Kinetics; D010673:Pheochromocytoma / Q000378:metabolism; D051381:Rats; D017461:Receptors, Atrial Natriuretic Factor; D011956:Receptors, Cell Surface / Q000378:metabolism*
D011956:Receptors, Cell Surface; D009320:Atrial Natriuretic Factor; D017461:Receptors, Atrial Natriuretic Factor