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Hypertension. 2007;49:765-766
Published online before print February 19, 2007, doi: 10.1161/01.HYP.0000258567.67263.96
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(Hypertension. 2007;49:765.)
© 2007 American Heart Association, Inc.


Editorial Commentaries

Natriuretic Peptides and Myocardial Structure

Insights From Population Genetics

John C. Burnett, Jr; Timothy M. Olson

From the Cardiorenal Research Laboratory (J.C.B.) and Cardiovascular Genetics Laboratory (T.M.O.), Division of Cardiovascular Diseases, Mayo Clinic and Mayo Clinic College of Medicine, Rochester, Minn.

Correspondence to John C. Burnett, Jr, Cardiorenal Research Laboratory, Guggenheim 9, Mayo Clinic College of Medicine, 200 First St SW, Rochester, MN 55905. E-mail burnett.john@mayo.edu


An extract of the first 250 words of the full text is provided, because this article has no 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


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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 biological actions after binding to the naturetic peptide receptor A and generating the second messenger cGMP. Superscript represents relevant references.

The work of Rame et al3 associating a corin polymorphism with ventricular hypertrophy in blacks builds on evidence of the importance of the natriuretic . . . [Full Text of this Article]


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Corin I555(P568) Allele Is Associated With Enhanced Cardiac Hypertrophic Response to Increased Systemic Afterload
J. Eduardo Rame, Mark H. Drazner, Wendy Post, Ronald Peshock, Joao Lima, Richard S. Cooper, and Daniel L. Dries
Hypertension 2007 49: 857-864. [Abstract] [Full Text] [PDF]



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X. Liao, W. Wang, S. Chen, and Q. Wu
Role of Glycosylation in Corin Zymogen Activation
J. Biol. Chem., September 21, 2007; 282(38): 27728 - 27735.
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