Colocalization of Somatostatin Receptor sst5 and Insulin in Rat Pancreatic β-Cells1

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...

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Veröffentlicht in:Endocrinology (Philadelphia) 1999-08, Vol.140 (8), p.3790-3796
Hauptverfasser: Mitra, Sudha Warrier, Mezey, Éva, Hunyady, Bela, Chamberlain, LaShawn, Hayes, Edward, Foor, Forrest, Wang, Yining, Schonbrunn, Agnes, Schaeffer, James M
Format: Artikel
Sprache:eng
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Zusammenfassung: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 β-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.
ISSN:0013-7227
1945-7170
DOI:10.1210/endo.140.8.6937