Cosecretion of amylin and insulin from isolated rat pancreas
HC Fehmann, V Weber, R Göke, B Göke, R Arnold - FEBS letters, 1990 - Elsevier
HC Fehmann, V Weber, R Göke, B Göke, R Arnold
FEBS letters, 1990•ElsevierAmylin, a 37 amino acid C-terminal amidated peptide is an integral part of secretory
granules of pancreatic β-cells. Utilizing a specific radioimmunoassay system we
demonstrate in the present study a cosecretion of amylin and insulin from the isolated rat
pancreas. The secretion pattern of both peptides during glucose or glucose plus arginine
stimulation is identical. The molar ratio of amylin amounts to 10% of that of insulin. The
biological significance of amylin is still unknown, but a paracrine/endocrine role in glucose …
granules of pancreatic β-cells. Utilizing a specific radioimmunoassay system we
demonstrate in the present study a cosecretion of amylin and insulin from the isolated rat
pancreas. The secretion pattern of both peptides during glucose or glucose plus arginine
stimulation is identical. The molar ratio of amylin amounts to 10% of that of insulin. The
biological significance of amylin is still unknown, but a paracrine/endocrine role in glucose …
Abstract
Amylin, a 37 amino acid C-terminal amidated peptide is an integral part of secretory granules of pancreatic β-cells. Utilizing a specific radioimmunoassay system we demonstrate in the present study a cosecretion of amylin and insulin from the isolated rat pancreas. The secretion pattern of both peptides during glucose or glucose plus arginine stimulation is identical. The molar ratio of amylin amounts to 10% of that of insulin. The biological significance of amylin is still unknown, but a paracrine/endocrine role in glucose homeostasis is speculated.
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