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

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71 Scopus citations


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, CGA(1-40 (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 bath exhibit saturable binding in an aortic smooth muscle cell line, indicative of a single class of high affinity binding protein ('receptor' with an apparent K, 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
Issue number1
StatePublished - 1994


  • Chromogranin A
  • Smooth muscle
  • Vasoconstriction

ASJC Scopus subject areas

  • Physiology


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