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Mutation of three amino acids in the disulfide-ring of a CNP based chimeric natriuretic peptide alters its vascular properties by Horng H Chen; Brenda K Huntley; Alessandro Cataliotti; Fernando L Martin; John C Burnett is a Medicine article available to read on EtoBox.

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## Clinical background C-type natriuretic peptide (CNP) is a 22-amino-acid peptide produced mainly in the endothelium with potent cardiac unloading and blood pressure lowering actions, but minimal renal actions. Based on our previous knowledge, we recently fused a 6 aa sequence from BNP to the C-terminus and a 5 aa sequence from ANP to the N-terminus of CNP. This novel hybrid peptide, CBA-NP, has cardiac unloading actions and mild hypotensive effects similar to CNP. Importantly however, the N and C terminus alterations resulted in potent renal excretory actions. Here we test the hypothesis that the 3 aa GSM 15-17 in the disulfidering mediate the vascular and hypotensive actions of CBA-NP. We therefore mutated GSM 15-17 to REA 15-17 , which we named ABC-NP and compared its in vivo and in vitro actions to CBA-NP.

Who reads Mutation of three amino acids in the disulfide-ring of a CNP based chimeric natriuretic peptide alters its vascular properties?

Author

Horng H Chen; Brenda K Huntley; Alessandro Cataliotti; Fernando L Martin; John C Burnett

Publisher

BioMed Central; Springer (Biomed Central Ltd.); London: BioMed Central, 2001-2012.; Springer Science and Business Media LLC (ISSN 1471-2210)

Published

2009

Language

EN

Field

Medicine (Life Sciences)