C-type natriuretic peptide in bovine chromaffin cells. The regulation of its biosynthesis and secretion

FEBS Lett. 1992 Nov 30;313(3):300-2. doi: 10.1016/0014-5793(92)81214-7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adrenal Medulla / metabolism*
  • Animals
  • Atrial Natriuretic Factor / metabolism
  • Cattle
  • Cells, Cultured
  • Chromatography, High Pressure Liquid
  • Colforsin / pharmacology
  • In Vitro Techniques
  • Natriuretic Peptide, C-Type
  • Nerve Tissue Proteins / metabolism*
  • Protein Kinase C / metabolism
  • Protein Kinases / metabolism
  • Protein Precursors / metabolism
  • Tetradecanoylphorbol Acetate / pharmacology

Substances

  • Nerve Tissue Proteins
  • Protein Precursors
  • Natriuretic Peptide, C-Type
  • Colforsin
  • Atrial Natriuretic Factor
  • Protein Kinases
  • Protein Kinase C
  • Tetradecanoylphorbol Acetate