Regulation of cholecystokinin secretion by calcium-dependent calmodulin kinase II: differential effects of phenylalanine and cAMP.

Published

Journal Article

The release of cholecystokinin was investigated in STC-1 cells, an intestinal cholecystokinin-secreting cell line. Fifteen minute incubation of cells with the amino acid, L-phenylalanine (20 mM), or the phosphodiesterase inhibitor, IBMX (100 microM), stimulated cholecystokinin secretion. Stimulation of secretion by both agents was associated with an increase in cytosolic calcium and was inhibited by the calcium channel blocker, diltiazem (10 microM). The calcium-calmodulin kinase II inhibitor, KN-65 (1.4 microM), markedly reduced IBMX-stimulated secretion, but had no effect on phenylalanine-mediated activity. KN-62 also inhibited IBMX-induced increases in cytosolic calcium, suggesting that cAMP may activate diltiazem-sensitive calcium channels by a calmodulin-dependent process.

Full Text

Duke Authors

Cited Authors

  • Prpic, V; Basavappa, S; Liddle, RA; Mangel, AW

Published Date

  • June 30, 1994

Published In

Volume / Issue

  • 201 / 3

Start / End Page

  • 1483 - 1489

PubMed ID

  • 7517671

Pubmed Central ID

  • 7517671

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1994.1871

Language

  • eng

Conference Location

  • United States