Published online before print April 23, 2007, doi: 10.1161/HYPERTENSIONAHA.106.069153
(Hypertension. 2007;50:25.)
© 2007 American Heart Association, Inc.
Hypertension Highlights |
Natriuretic Peptides
Update on Peptide Release, Bioactivity, and Clinical Use
From the Department of Medicine, Christchurch School of Medicine and Health Sciences, Christchurch, New Zealand.
Correspondence to Professor A. Mark Richards, National Heart Foundation (New Zealand) Professor of Cardiovascular Studies, Department of Medicine, Christchurch School of Medicine and Health Sciences (University of Otago), PO Box 4345, Christchurch, New Zealand. E-mail mark.richards@cdhb.govt.nz
An extract of the first 250 words of the full text is provided, because this article has no abstract. |
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Introduction |
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In the 25 years since de Bold et al demonstrated the existence of an atrial natriuretic factor, investigation of the cardiac natriuretic peptides has produced a maturing knowledge base1,2 identifying the cardiac peptides and addressing stimuli for secretion of atrial (ANP) and B-type (BNP) natriuretic peptides, the processing and release of the mature bioactive carboxy terminal peptides, together with their propeptides and amino terminal fragments, the nature of natriuretic peptide receptors, and the bioactivities of natriuretic peptides (including natriuresis, vasodilatation, suppression of renin–angiotensin–aldosterone and sympathetic nervous activity, and trophic effects inhibiting vascular and cardiac hypertrophy and fibrosis). Less is known of the more recently discovered C-type natriuretic peptide (CNP and its cosecreted amino-terminal peptide, NTproCNP).3,4 Increasingly, measurements of the B-type peptides have found diagnostic and prognostic application in cardiovascular disease.5–7
The genes for ANP and BNP are in tandem on human chromosome 1.8 Upstream regulatory regions identified for the BNP gene include an AP1 binding site, serum response elements, M-CAT and GATA sites.9,10 Translation results in pre-pro BNP from which a 26 amino acid signal peptide is cleaved to produce the 108 amino acid precursor proBNP. This in turn is processed between amino acid residues 76 and 77 resulting in a 32 amino acid biologically active peptide (BNP) from its carboxy terminal plus the remaining amino terminal peptide sequence (NTproBNP 1 to 76). ANP is synthesized as a 126 amino acid precursor and is stored in granules within atrial tissue.11 During or shortly after secretion, the precursor is processed to
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