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Enzymatic Inactivation of Major Circulating Forms of Atrial and Brain Natriuretic Peptides

Enzymatic Inactivation of Major Circulating Forms of Atrial and Brain Natriuretic Peptides

J Ozaki, H Shimizu, Y Hashimoto, H Itoh, K Nakao, K Inui

Eur J Pharmacol. 1999 Apr 16;370(3):307-12.

PMID: 10334507

Abstract:

We compared the enzymatic inactivation of major circulating forms of atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). Both ANP and BNP induced a significant increase in cyclic GMP (cGMP) formation in cultured epithelial cell line derived from porcine kidney, LLC-PK1. The cGMP formation stimulated by ANP in LLC-PK1 cells was significantly decreased by pre-treatment of the peptide with rat renal brush-border membranes, and the inactivation of ANP was inhibited by neutral endopeptidase inhibitors, phosphoramidon and S-thiorphan. BNP exhibited greater resistance to enzymatic inactivation than did ANP. In addition, phosphoramidon potentiated the natriuresis with a low dose (7.5 pmol min(-1) kg(-1)) of ANP but not of BNP in rats. These results suggest that enzymatic degradation of natriuretic peptides is highly dependent on peptide structure, and that the affinity of BNP to neutral endopeptidase is less than that of ANP.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42412318	Endopeptidase, Neutral, Porcine Kidney			Price

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