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J Biol Chem, Vol. 273, Issue 37, 24173-24180, September 11, 1998
From the Departments of Cholecystokinin (CCK) and other
pancreatic secretagogues have recently been shown to activate signaling
kinase cascades in pancreatic acinar cells, leading to the activation
of extracellular signal-regulated kinases and Jun N-terminal kinases.
We now show the presence of a third kinase cascade activating p38
mitogen-activated protein (MAP) kinase in isolated rat pancreatic
acini. CCK and osmotic stress induced by sorbitol activated p38 MAP
kinase within minutes; their effects were dose-dependent,
with maximal activation of 2.8- and 4.4-fold, respectively. The effects
of carbachol and bombesin on p38 MAP kinase activity were similar to
those of CCK, whereas phorbol ester, epidermal growth factor, and
vasoactive intestinal polypeptide stimulated p38 MAP kinase by 2-fold
or less. Both CCK and sorbitol also increased the tyrosyl
phosphorylation of p38 MAP kinase. Using the specific inhibitor of p38
MAP kinase, SB 203580, we found that p38 MAP kinase activity was
required for MAP kinase-activated protein kinase-2 activation in
pancreatic acini. SB 203580 reduced the level of basal phosphorylation
and blocked the increased phosphorylation of Hsp 27 after stimulation with either CCK or sorbitol. CCK treatment induced an initial rapid
decrease in total F-actin content of acini, followed by an increase
after 40 min. Preincubation with SB 203580 significantly inhibited
these changes in F-actin content. Staining of the actin cytoskeleton
with rhodamine-conjugated phalloidin and analysis by confocal
fluorescence microscopy showed disruption of the actin cytoskeleton
after 10 and 40 min of CCK stimulation. Pretreatment with SB 203580 reduced these changes. These findings demonstrate that the activation
of p38 MAP kinase is involved not only in response to stress, but also
in physiological signaling by gastrointestinal hormones such as CCK,
where activation of Gq-coupled receptors stimulates a
cascade in which p38 MAP kinase activates MAP kinase-activated protein
kinase-2, resulting in Hsp 27 phosphorylation. Activation of p38 MAP
kinase, most likely through phosphorylation of Hsp 27, plays a role in
the organization of the actin cytoskeleton in pancreatic acini.
A Role for the p38 Mitogen-activated Protein Kinase/Hsp 27 Pathway in Cholecystokinin-induced Changes in the Actin Cytoskeleton in
Rat Pancreatic Acini
,,,,
Physiology and Internal
Medicine and ¶ Anatomy and Cell Biology, University of Michigan,
Ann Arbor, Michigan 48109-0622
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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