Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets.

作者: A. Lukinius , E. Wilander , G. T. Westermark , U. Engstr�m , P. Westermark

DOI: 10.1007/BF00285291

关键词:

摘要: Islet amyloid polypeptide is a novel 37 amino-acid-residues which has been isolated from deposits in an insulinoma, and human cat islets of Langerhans. The molecule 46% homology with the calcitonin gene-related peptide. Light microscopy examination pancreas shows that islet immunoreactivity restricted to B cells. present study utilized rabbit antiserum against synthetic peptide corresponding positions 20–29 polypeptide, sequence without any amino-acid identity By applying immunogold technique at ultrastructural level, it was shown both insulin occurs central granular core cell secretory granules, while A cells remain unlabelled. demonstration protein may indicate released together insulin. Further studies are necessary evaluate functional role polypeptide.

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