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 journalArticle

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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, 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
Volume152
Issue number1
StatePublished - 1994

Fingerprint

Chromogranin A
Endothelin-1
Peptides
Smooth Muscle Myocytes
Calcium
Calcium-Binding Proteins
Saphenous Vein
Secretory Vesicles
Baths
Endothelium
Norepinephrine
Potassium
Carrier Proteins
Cell Line
vasostatin I

Keywords

  • Chromogranin A
  • Smooth muscle
  • Vasoconstriction

ASJC Scopus subject areas

  • Physiology

Cite this

Angeletti, R. H., Aardal, S., Serck-Hanssen, G., Gee, P., & Helle, K. B. (1994). Vasoinhibitory activity of synthetic peptides from the amino terminus of chromogranin A. Acta Physiologica Scandinavica, 152(1), 11-19.

Vasoinhibitory activity of synthetic peptides from the amino terminus of chromogranin A. / Angeletti, R. H.; Aardal, S.; Serck-Hanssen, G.; Gee, P.; Helle, K. B.

In: Acta Physiologica Scandinavica, Vol. 152, No. 1, 1994, p. 11-19.

Research output: Contribution to journalArticle

Angeletti, RH, Aardal, S, Serck-Hanssen, G, Gee, P & Helle, KB 1994, 'Vasoinhibitory activity of synthetic peptides from the amino terminus of chromogranin A', Acta Physiologica Scandinavica, vol. 152, no. 1, pp. 11-19.
Angeletti RH, Aardal S, Serck-Hanssen G, Gee P, Helle KB. Vasoinhibitory activity of synthetic peptides from the amino terminus of chromogranin A. Acta Physiologica Scandinavica. 1994;152(1):11-19.
Angeletti, R. H. ; Aardal, S. ; Serck-Hanssen, G. ; Gee, P. ; Helle, K. B. / Vasoinhibitory activity of synthetic peptides from the amino terminus of chromogranin A. In: Acta Physiologica Scandinavica. 1994 ; Vol. 152, No. 1. pp. 11-19.
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