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Control of somatostatin (SS) secretion by CCK-1 and CCK-2 receptors' occupation in RIN-14B cells, a rat pancreatic

Karim El-Kouhen1, Jean Morisset

  • 1Faculty of Medicine, Department of Medicine, Université de Sherbrooke, Sherbrooke, Quebec, Canada.

Pancreas
|December 5, 2009
PubMed
Abstract

Insights

Cholecystokinin (CCK) receptors on RIN-14B cells stimulate somatostatin (SS) secretion. Both CCK receptor subtypes initiate SS release via constitutive secretion, with CCK-1R occupation mobilizing high-affinity sites.

Area of Science:

  • Endocrinology
  • Cell Biology
  • Gastroenterology

Background:

  • Somatostatin (SS) plays a crucial role in regulating various physiological processes.
  • Cholecystokinin (CCK) receptors are implicated in modulating hormone secretion.
  • Understanding the interplay between CCK receptors and SS secretion is vital for endocrine research.

Purpose of the Study:

  • To investigate the role of cholecystokinin (CCK) receptor occupation in controlling somatostatin (SS) secretion in RIN-14B cells.
  • To elucidate the specific CCK receptor subtypes involved in SS release.
  • To determine the mechanism of SS secretion stimulated by CCK receptor activation.

Main Methods:

  • Immunofluorescence was used to confirm the presence of CCK receptor subtypes 1 and 2 (CCK-R1, CCK-R2) in RIN-14B cells.
  • Enzyme-linked immunosorbent assay (ELISA) was employed to quantify SS secretion.
  • Specific CCK receptor agonists (cerulein, pentagastrin) and antagonists (L-364,178, L-365,260) were utilized to assess receptor function.

Main Results:

  • RIN-14B cells predominantly comprise SS cells (95%) expressing both CCK-R1 and CCK-R2.
  • CCK-R1 and CCK-R2 agonists dose-dependently increased SS release.
  • Constitutive secretion accounts for over 60% of SS release, regulated at the synthesis level.

Conclusions:

  • Both CCK receptor subtypes are present on RIN-14B cells and mediate SS secretion.
  • SS secretion is initiated through a constitutive pathway regulated by SS synthesis.
  • CCK-1R occupation specifically mobilizes high-affinity CCK-1R sites to enhance SS release.

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