Colocalization of Somatostatin Receptor sst5 and Insulin in Rat Pancreatic ß-Cells
Sudha Warrier Mitra; Éva Mezey; Bela Hunyady; LaShawn Chamberlain; Edward Hayes; Forrest Foor; Yining Wang; Agnes Schonbrunn and James M. Schaeffer
05/22/2014
Endocrinology
Somatostatin, also known as somatotropin release-inhibiting factor (SRIF), is secreted by pancreatic δ-cells and inhibits the secretion of both insulin and glucagon. SRIF initiates its actions by binding to a family of six G protein-coupled receptors (sst1, -2A, -2B, -3, -4, and -5) encoded by five genes. Messenger RNA for both sst2 and sst5 have been reported in the rat pancreas, and the sst2A receptor protein has been localized to rat pancreatic α and pancreatic polypeptide-secreting cells in the islets as well as to pancreatic acinar cells. In this study we have used double immunostaining to show that the sst5 protein is expressed exclusively in the ß-cells of rat pancreatic islets and localizes with insulin-secreting α-cells. The sst5 receptor is not colocalized with sst2A. Thus, in the rat SRIF inhibits pancreatic insulin and glucagon secretion via different sst receptor subtypes. (Endocrinology 140: 3790–3796, 1999)