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Oxyntomodulin and related peptides control somatostatin secretion in RIN T3 cells

T Tani1, A Le Quellec, C Jarrousse

  • 1Centre CNRS-INSERM de Pharmacologie-Endocrinologie, Montpellier, France.

Insights

Oxyntomodulin (OXM) and glucagon stimulate somatostatin release and cyclic AMP in RIN T3 cells. A separate pathway involving the OXM (19-37) fragment also triggers somatostatin release.

Area of Science:

  • Endocrinology
  • Cell Biology
  • Molecular Pharmacology

Background:

  • Somatostatin plays a crucial role in regulating gastric acid secretion and other physiological processes.
  • RIN T3 cells are a well-established model for studying pancreatic islet cell function and hormone secretion.

Purpose of the Study:

  • To investigate the effects of oxyntomodulin (OXM), its C-terminal fragment (OXM (19-37)), and glucagon (GLU) on somatostatin release in RIN T3 cells.
  • To elucidate the signaling pathways involved, including cyclic AMP accumulation, inositol phosphate turnover, and intracellular calcium changes.
  • To compare the actions of these peptides with carbachol, a known activator of the inositol phosphate/Ca2+ cascade.

Main Methods:

  • Cultured RIN T3 cells were treated with OXM, OXM (19-37), GLU, and carbachol.
  • Somatostatin release was measured.
  • Cyclic AMP accumulation was assessed.
  • Inositol phosphate turnover and intracellular free Ca2+ levels were monitored using fura-2.

Main Results:

  • OXM, GLU, and OXM (19-37) all stimulated somatostatin release, with OXM being the most potent.
  • OXM and GLU increased cyclic AMP levels, while OXM (19-37) had no effect.
  • None of the tested peptides affected inositol phosphate turnover or induced rapid changes in intracellular Ca2+, unlike carbachol.

Conclusions:

  • RIN T3 cells possess a receptor-cyclic AMP system linked to somatostatin release, similar to that in gastric mucosa.
  • A distinct receptor-second messenger mechanism, not involving the inositol phosphate/Ca2+ cascade, mediates somatostatin release stimulated by the OXM (19-37) fragment.

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