Vasoinhibitory activity of synthetic peptides from the amino terminus of chromogranin A

R. H. ANGELETTI, S. AARDAL, G. SERCK‐HANSSEN, P. GEE, K. B. HELLE

Research output: Contribution to journalArticlepeer-review

71 Scopus citations

Abstract

Naturally occurring amino terminal fragments of chromogranin A (CGA), the calcium‐binding protein found in all endocrine secretory vesicles, have vasoinhibitory activity when tested in isolated segments of the endothelium‐denuded human saphenous vein. Synthetic peptides corresponding to sequences within the first 76 residues of chromogranin A have been made and tested for biological activity. Full length vasostatin I (CGA1–76) (40 nM), but not the truncated vasostatin I, CGA1–40 (100 nM) mimics natural chromogranin A fragments in its inhibition of contractions induced by endothelin‐1 (ET‐1) in calcium containing medium. CGA1–40 (100 nM) mimics the inhibitory effect of the vasostatins on the contractions induced in the absence of extracellular calcium by high potassium and noradrenaline, but not by ET‐1. The iodinated peptides both exhibit saturable binding in an aortic smooth muscle cell line, indicative of a single class of high affinity binding protein (‘receptor’ with an apparent KD of approximately 45 nM. This binding is not affected by endothelin‐1. Iodinated peptides can be crosslinked to a single polypeptide in binding experiments performed on intact calf aortic smooth muscle cells.

Original languageEnglish (US)
Pages (from-to)11-19
Number of pages9
JournalActa Physiologica Scandinavica
Volume152
Issue number1
DOIs
StatePublished - Sep 1994

Keywords

  • chromogranin A
  • smooth muscle
  • vasoconstriction

ASJC Scopus subject areas

  • Physiology

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