Molecular forms of immunoactive atrial natriuretic peptide in the rat hypothalamus and atrium.
Acid extracts of rat hypothalamus and atrium were prepared by a procedure previously shown to minimize proteolytic degradation of peptides. The majority of the immunoactive material in the atrial extracts had a molecular weight of approximately 9,000 to 15,000 daltons, while that in the hypothalamic extracts had a molecular weight of about 1,500 to 1,800 daltons. The major molecular weight forms of atrial natriuretic peptide from each extract were further distinguishable when analyzed by RP-HPLC. These results suggest that small peptides such as atriopeptins I, II, and III, may not be authentic post-translational processing products in the atrium, and that the hypothalamus and atrium may differentially cleave pro-atrial natriuretic peptide to form tissue-specific products.
Glembotski
C C
CC
Wildey
G M
GM
Gibson
T R
TR
D000818:Animals; D009320:Atrial Natriuretic Factor; D002851:Chromatography, High Pressure Liquid; D006325:Heart Atria / Q000032:analysis; D007031:Hypothalamus / Q000032:analysis*; D008970:Molecular Weight; D009124:Muscle Proteins / Q000032:analysis*; D009206:Myocardium / Q000032:analysis*; D011499:Protein Processing, Post-Translational; D011863:Radioimmunoassay; D051381:Rats
D009124:Muscle Proteins; D009320:Atrial Natriuretic Factor