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J Biol Chem, Vol. 274, Issue 34, 23901-23909, August 20, 1999
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From the Departments of Gastrin-releasing peptide (GRP) and its amphibian
homolog, bombesin, are potent secretogogues in mammals. We determined
the roles of intracellular free Ca2+
([Ca2+]i), protein kinase C
(PKC), and mitogen-activated protein kinases (MAPK) in GRP receptor
(GRP-R)-regulated secretion. Bombesin induced either
[Ca2+]i oscillations or a
biphasic elevation in [Ca2+]i.
The biphasic response was associated with peptide secretion.
Receptor-activated secretion was blocked by removal of extracellular
Ca2+, by chelation of
[Ca2+]i, and by treatment with
inhibitors of phospholipase C, conventional PKC isozymes, and MAPK
kinase (MEK). Agonist-induced increases in
[Ca2+]i were also inhibited by
dominant negative MEK-1 and the MEK inhibitor, PD89059, but not by
an inhibitor of PKC. Direct activation of PKC by a phorbol ester
activated MAPK and stimulated peptide secretion without a concomitant
increase in [Ca2+]i. Inhibition
of MEK blocked both bombesin- and phorbol 12-myristate
13-acetate-induced secretion. GRP-R-regulated secretion is initiated by
an increase in [Ca2+]i; however,
elevated [Ca2+]i is insufficient
to stimulate secretion in the absence of activation of PKC and the
downstream MEK/MAPK pathways. We demonstrated that the activity of MEK
is important for maintaining elevated
[Ca2+]i levels induced by GRP-R
activation, suggesting that MEK may affect receptor-regulated secretion
by modulating the activity of Ca2+-sensitive PKC.
Surgery, Physiology
and Biophysics, and ¶ Obstetrics and Gynecology, University of
Texas Medical Branch, Galveston, Texas 77555
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