Purification and Sequence Analysis of Bioactive Atrial Peptides (Atriopeptins)

• Published in: Science (American Association for the Advancement of Science) 1984-01, Vol.223 (4631), p.67-69
• Main Authors: Currie, Mark G., Geller, David M., Cole, Barbara R., Siegel, Ned R., Fok, Kam F., Adams, Steven P., Eubanks, Shad R., Galluppi, Gerald R., Needleman, Philip
• Format: Article
• Language: English
• Subjects: Acetates; Amino Acid Sequence; Amino acids; Aminoacids, peptides. Hormones. Neuropeptides; Analysis; Analytical, structural and metabolic biochemistry; Animals; Aorta; Arginine - analysis; atriopeptin; atrium; Biochemistry; Biological and medical sciences; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Diuresis - drug effects; Diuretics; Excretion; Fundamental and applied biological sciences. Psychology; Glycine - analysis; Heart Atria - analysis; Low molecular weights; mammals; Muscle Contraction - drug effects; Muscle, Smooth - drug effects; Muscle, Smooth, Vascular - drug effects; Natriuresis - drug effects; Peptides; Peptides - analysis; Peptides - isolation & purification; Peptides - pharmacology; Pharmacological research; Pharmacology, Experimental; Phenylalanine - analysis; Proteins; Rats; Rectum; Sequence analysis; Serine - analysis; Smooth muscle; Sodium
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.6419347

Mammalian cardiac atria have several biologically active peptides that exert profound effects on sodium excretion, urine volume, and smooth muscle tone. In the present study two such peptides of low molecular weight were purified and separated from each other on the basis of differences in charge, hydrophobicity, and biological profile. The first peptide, designated atriopeptin I, exhibits natriuretic and diuretic activity and selectivity relaxes intestinal smooth muscle but not vascular smooth muscle strips. The second peptide, atriopeptin II, is a potent natriuretic and diuretic that relaxes both intestinal and vascular strips. Sequence analysis of atriopeptin I indicates that it is composed of 21 amino acids, of which serine and glycine residues predominate. The amino terminal sequence of atriopeptin II up to residue 21 is the same as that of atriopeptin I, with the addition of the Phe-Arg extension at the carboxyl terminus. Both peptides appear to be derived from a common high molecular weight precursor (designated atriopeptigen); their biological selectivity and potency may be determined by the site of carboxyl terminal cleavage.