title: Receptors for atrial natriuretic peptide in adrenal chromaffin cells.
abstract: Receptors for atrial natriuretic peptide (ANP) in isolated bovine adrenal chromaffin cells were characterized. 125 I-ANP specifically bound to the cells with a Kd of 103 pM and a Bmax of 5.6 fmol/10(6) cells (16.5 fmol/mg of cell protein). C-ANF, a highly selective ligand for ANP-C receptors of natriuretic peptides, did not compete for 125 I-ANP binding at concentrations up to 10nM. Chemical cross-linking of 125I-ANP to the cells showed a single molecular size of the 120 kDa binding site on SDS gel electrophoresis under reducing conditions. CNP, a specific peptide for the ANP-B receptor, was much less potent than ANP in inhibiting 125 I-ANP binding and in displacing 125 I-ANP from the 120 kDa band. These results suggest that ANP specifically binds to the ANP-A receptor of 120 kDa and that there is no ANP-C receptor in bovine adrenal chromaffin cells.
authors.affiliation: Department of Pharmacology, Miyazaki Medical College, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Niina
authors.forename: H
authors.initials: H
authors.lastname: Kobayashi
authors.forename: R
authors.initials: R
authors.lastname: Yamamoto
authors.forename: T
authors.initials: T
authors.lastname: Yuhi
authors.forename: T
authors.initials: T
authors.lastname: Yanagita
authors.forename: A
authors.initials: A
authors.lastname: Wada
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D009320:Atrial Natriuretic Factor / Q000378:metabolism; D001665:Binding Sites; D002417:Cattle; D002478:Cells, Cultured; D002838:Chromaffin System / Q000648:ultrastructure*; D006152:Cyclic GMP / Q000096:biosynthesis; D006801:Humans; D007457:Iodine Radioisotopes; D007700:Kinetics; D008969:Molecular Sequence Data; D017461:Receptors, Atrial Natriuretic Factor / Q000378:metabolism*
chemical_list: D007457:Iodine Radioisotopes; D009320:Atrial Natriuretic Factor; D017461:Receptors, Atrial Natriuretic Factor; D006152:Cyclic GMP