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

@article{Angeletti1994VasoinhibitoryAO,
  title={Vasoinhibitory activity of synthetic peptides from the amino terminus of chromogranin A.},
  author={R H Angeletti and Sidsel Aardal and Guldborg Serck-Hanssen and Peter Gee and Karen B. Helle},
  journal={Acta physiologica Scandinavica},
  year={1994},
  volume={152 1},
  pages={
          11-9
        }
}
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… CONTINUE READING
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