Mammalian bombesin receptors are coupled to multiple signal transduction pathways in pancreatic acini

The American Journal of Physiology
H NishinoC Owyang

Abstract

We investigated the structural requirements for bombesin (BB)-like peptides to stimulate amylase secretion in rat pancreatic acini and examined the responsible intracellular signal transduction pathways. The tetradecapeptide BB-(1-14) was a full agonist, whereas the heptapeptide BB-(8-14) did not evoke amylase secretion. The mammalian BB analog neuromedin C decapeptide [NMC-(5-14)] was as potent as BB-(1-14) in stimulating amylase secretion, suggesting that Gly5-Asn6-His7 (or Gln7) of the COOH-terminal decapeptide are essential amino acids for full biological activity. BB and NMC equipotently stimulated D-myo-inositol 1,4,5-trisphosphate production, which was inhibited by the phospholipase C (PLC) inhibitor U-73122. BB and NMC also stimulated protein tyrosine kinase (PTK) activities. The half-maximal effective concentration (EC50) for NMC-activated PTK was 2 log units less than the EC50 for BB-activated PTK. NMC was 10-34 times more potent than BB in increasing leukotriene C4 (an index of arachidonic acid production). The production of leukotriene C4 was inhibited by the phospholipase A2 (PLA2) inhibitor ONO-RS-082. NMC is structurally homologous to BB-(5-14) except that Gln7 in BB is replaced by His7 in NMC. Therefore, substit...Continue Reading

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Citations

Jul 27, 2000·American Journal of Physiology. Cell Physiology·H J KimC M Townsend
Aug 19, 2011·American Journal of Physiology. Regulatory, Integrative and Comparative Physiology·Branimir Zogovic, Paul M Pilowsky
Sep 2, 2008·Langmuir : the ACS Journal of Surfaces and Colloids·Edyta PodstawkaLeonard M Proniewicz
Mar 20, 2009·The Journal of Physical Chemistry. B·Edyta Podstawka, Leonard M Proniewicz

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