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1: Biochem Biophys Res Commun. 1991 Mar 15;175(2):645-51.Click here to read Links

Gene and precursor structures of human C-type natriuretic peptide.

Tawaragi Y, Fuchimura K, Tanaka S, Minamino N, Kangawa K, Matsuo H.

Suntory Institute for Biomedical Research, Osaka, Japan.

We have isolated the gene for human C-type natriuretic peptide (CNP) from a human genomic library using a cloned porcine CNP genomic DNA fragment as probe. Human CNP gene consists of at least two coding blocks and an intron, and encodes a 126-residue CNP precursor (human prepro-CNP). From a comparison of the amino acid sequences of porcine and rat prepro-CNPs, human prepro-CNP is found to be processed to generate 22-and 53-residue peptides (human CNP-22 and human CNP-53, respectively) as major endogenous CNPs in human. Interestingly, human CNP-53 has two amino acid substitutions as compared to the porcine and rat CNP-53s, whereas human CNP-22 is identical to the porcine and rat CNP-22s. Intravenous injection of human CNP-53 into anesthetized rats induces diuretic-natriuretic and hypotensive activities with same potencies as porcine CNP-53 does, although these activities were considerably lower (about 1/100) than those of human alpha-ANP.

PMID: 2018508 [PubMed - indexed for MEDLINE]