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C‐type natriuretic peptide in bovine chromaffin cells The regulation of its biosynthesis and secretion
Author(s) -
Babinski K.,
Féthière J.,
Roy M.,
De Léan A.,
Ong H.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81214-7
Subject(s) - secretion , natriuretic peptide , intracellular , biosynthesis , medicine , npr1 , atrial natriuretic peptide , endocrinology , peptide , stimulation , neurotransmitter , chromaffin cell , depolarization , chemistry , npr2 , biology , microbiology and biotechnology , biochemistry , catecholamine , adrenal medulla , enzyme , central nervous system , heart failure
We report here the regulation of the biosynthesis and the secretion of C‐type natriuretic peptide (CNP) in cultured bovine chromaffin cells. The combined treatment with protein kinase A and ‐C activators induced a 6‐fold increase of intracellular levels of CNP‐(1–103). The biosynthesized CNP‐(1–103) was co‐released with its mature forms, typically CNP‐(51–103), upon stimulation by nicotine or depolarizing agents. This confirms the neuropeptidic character of this third member of the natriuretic peptide family, which might act as a neuromodulator or neurotransmitter.