Inhibition of insulin secretion by betagranin, an N-terminal chromogranin A fragment

J Biol Chem. 2007 Apr 27;282(17):12717-24. doi: 10.1074/jbc.M700788200. Epub 2007 Feb 8.

Abstract

Betagranin, an N-terminal fragment of chromogranin A, results from a proteolytic processing, and is co-secreted with insulin. While other chromogranin A-derived peptides negatively modulate hormone secretion, the role of betagranin in pancreatic beta-cells is so far unknown. We have recently shown that pancreatic islet betagranin levels are down-regulated in obese, leptin-deficient mice. In the present study, we have investigated the distribution of betagranin in primary mouse islets and cells of the MIN6 line and have evaluated its effects on insulin secretion. We showed that betagranin co-localizes with insulin within secretory granules and strongly inhibited insulin secretion in response to both glucose and potassium, by blocking the influx of calcium. The data demonstrated a hitherto unknown inhibitory effect of betagranin on insulin secretion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcium Signaling / drug effects*
  • Cell Line
  • Chromogranins / pharmacology*
  • Female
  • Glucose / metabolism
  • Glucose / pharmacology
  • Insulin / metabolism*
  • Insulin Secretion
  • Islets of Langerhans / metabolism*
  • Islets of Langerhans / ultrastructure
  • Mice
  • Potassium / metabolism
  • Potassium / pharmacology
  • Sweetening Agents / pharmacology

Substances

  • Chromogranins
  • Insulin
  • Sweetening Agents
  • beta-granins
  • Glucose
  • Potassium