Identification of the receptor for atrial natriuretic factor on cultured vascular cells

Binding experiments with 125I-atrial natriuretic factor (ANF) followed by covalent attachment with disuccimidyl suberate show that the peptide binds predominantly to a protein of apparent molecular mass of 66,000 daltons on the cell surface of cultured bovine aortic smooth muscle cells. A minor prot...

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Bibliographic Details
Published in:The Journal of biological chemistry 1985-12, Vol.260 (28), p.14887-14890
Main Authors: Schenk, D B, Phelps, M N, Porter, J G, Scarborough, R M, McEnroe, G A, Lewicki, J A
Format: Article
Language:English
Subjects:
Angiotensin II - metabolism
Animals
Atrial Natriuretic Factor - metabolism
Autoradiography
Binding, Competitive
Biological and medical sciences
Cattle
Cell receptors
Cell structures and functions
Cells, Cultured
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Glucagon - metabolism
Insulin - metabolism
Molecular and cellular biology
Molecular Weight
Muscle, Smooth, Vascular - analysis
Receptors, Atrial Natriuretic Factor
Receptors, Cell Surface - analysis
Succinimides - pharmacology
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Summary:Binding experiments with 125I-atrial natriuretic factor (ANF) followed by covalent attachment with disuccimidyl suberate show that the peptide binds predominantly to a protein of apparent molecular mass of 66,000 daltons on the cell surface of cultured bovine aortic smooth muscle cells. A minor protein species of 180,000 Mr is also visualized after cross-linking. Endothelial cells, however, whose ANF binding parameters differ substantially from smooth muscle cells, also appear to have qualitatively identical 125I-ANF binding proteins. The identity of these putative proteins, as the ANF receptor, is confirmed by findings that covalent attachment of 125I-ANF is saturable, concentration-dependent, and competed by nanomolar concentrations of unlabeled ANF. Furthermore, other peptide hormones such as angiotensin II, glucagon, or insulin are ineffective in competing for 125I-ANF binding and cross-linking to the receptor.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)95674-7