Natriuretic Peptides and Myocardial Structure

Abstract

It has been more than 2 decades since the seminal report by DeBold demonstrating the existence of atrial natriuretic peptide (ANP) as a cardiac hormone that links the heart and kidney in cardiorenal homeostasis.1 Since that discovery, a family of structurally similar but genetically distinct peptides have been reported that function via well-characterized particulate guanylyl cyclase receptors linked to cGMP. These include ANP and B-type naturetic peptide (BNP), which are ligands for the naturetic peptide receptor A, and C-type naturetic peptide, which binds to the naturetic peptide receptor B.2 In the current issue, Rame et al3 focus attention on the processing of the cardiac peptide prohormones to mature biologically active peptides by the protease corin. This study was predicated by the work by Yan et al,4 which established corin as the natriuretic peptide-converting enzyme for ANP and presumably BNP (Figure). This cleavage of the prohormone to the mature peptide is essential for biological activity exemplified by a novel murine model of corin deletion in which the phenotype is hypertension and cardiac hypertrophy.5 Processing of pro-ANP and pro-BNP. This figure illustrates the processing of these 2 procardiac natriuretic peptides by corin to biologically active mature cardiac natriuretic peptides ANP and BNP. These peptides mediate their …