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Bimodal regulation of pancreatic exocrine function in vitro by somatostatin-28

Esteve, J. P. ; Vaysse, N. ; Susini, C. ; Kunsch, J. M. ; Fourmy, D. ; Pradayrol, L. ; Wunsch, E. ; Moroder, L. ; Ribet, A.

American journal of physiology: Gastrointestinal and liver physiology, , Vol.245 (2), p.G208-G216 [Periódico revisado por pares]

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  • Título:
    Bimodal regulation of pancreatic exocrine function in vitro by somatostatin-28
  • Autor: Esteve, J. P. ; Vaysse, N. ; Susini, C. ; Kunsch, J. M. ; Fourmy, D. ; Pradayrol, L. ; Wunsch, E. ; Moroder, L. ; Ribet, A.
  • É parte de: American journal of physiology: Gastrointestinal and liver physiology, , Vol.245 (2), p.G208-G216
  • Descrição: The action of natural and synthetic somatostatin-(1--28), [Nle8]somatostatin-(1--28), somatostatin-(15--28), and somatostatin-(1--14) was examined in dispersed acini from guinea pig pancreas. At high concentrations, the 28-amino acid form of somatostatin increased amylase release, outflux of 45Ca, cellular cGMP, and to a lesser extent cellular cAMP. The increase in amylase release was suppressed by dibutyryl cGMP but was not modified by theophylline or atropine. Binding of 125I-labeled [Thr28, Nle31] cholecystokinin-(25--33) was inhibited by [Nle8]somatostatin-(1--28). These effects required the entire 28-amino acid peptide and appeared to result from occupation of cholecystokinin receptors. It is postulated that they involve interactions between the C-terminal and the N-terminal sequences of the molecule with the participation of the amino acid in position 8. At low concentrations, natural and synthetic forms of somatostatin-(1--28) and somatostatin-(15--28) inhibited secretin- and vasoactive intestinal peptide (VIP)-stimulated increases in cellular cAMP concentration. No difference was found between the potency of somatostatin peptides, indicating that the tetradecapeptide somatostatin-(15--28) is sufficient to exert an inhibitory action on secretin- and VIP-stimulated cellular cAMP concentration. By contrast, the somatostatin fragment S-(1--14) was inactive on pancreatic cellular function.
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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