Differential Stimulation of Rat Lung Particulate Guanylate Cyclase Activity by Atrial Natriuretic Peptide and Sodium Nitroprusside

• Published in: Journal of biochemistry (Tokyo) 1989-05, Vol.105 (5), p.697-699
• Main Authors: Iwasa, Fuyuki, Furuya, Mayumi, Hayashi, Yujiro, Ohnuma, Norio
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Atrial Natriuretic Factor - metabolism; Atrial Natriuretic Factor - pharmacology; atrial natriuretic hormone; Biological and medical sciences; Diamide - pharmacology; Enzyme Activation; Enzymes and enzyme inhibitors; Ethylmaleimide - pharmacology; Ferricyanides - pharmacology; Fundamental and applied biological sciences. Psychology; guanylate cyclase; Guanylate Cyclase - metabolism; In Vitro Techniques; lung; Lung - enzymology; Lyases; Male; Nitroprusside - pharmacology; Protein Binding; Rats; Rats, Inbred Strains; Sulfhydryl Reagents - pharmacology
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/oxfordjournals.jbchem.a122729

The effects of α-rat atrial natriuretic peptide (α-rANP) and sodium nitroprusside on the activity of rat lung particulate guanylate cyclase were examined. The particulate guanylate cyclase in partially purified rat lung membranes was stimulated by both α-rANP and nitroprusside. The effects of α-rANP and nitroprusside were, however, not additive. Diamide and N-ethylmaleimide almost completely abolished the nitroprusside-mediated stimulation, while they had only moderate effects on the α-rANP-mediated stimulation of the enzyme activity. ATP potentiated the enzyme stimulation by α-rANP, whereas it had no effect on the nitroprusside-mediated stimulation. These findings suggest that the stimulation of lung particulate guanylate cyclase activity by α-rANP and nitroprusside is mediated by different mechanisms.