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(Received for publication, February 4, 1997, and in revised form, April 28, 1997)
From the Department of Pharmacology, University of Colorado Health
Sciences Center, Denver, Colorado 80262 and Denver Veteran Affairs
Medical Center, Denver, Colorado 80220
p38 is a member of the mitogen-activated protein
(MAP) kinase superfamily activated by stress signals and implicated in
cellular processes involving inflammation and apoptosis. Unlike the
extracellular signal-regulated kinases (p42 and p44 MAP kinases), which
are stimulated by insulin in many cell types, p38 activity is inhibited by insulin in postmitotic fetal neurons for which insulin is a potent
survival factor (Heidenreich, K. A., and Kummer, J. L. (1996)
J. Biol. Chem. 271, 9891-9894). These data suggested
that insulin's effects on neuronal survival are mediated by inhibition of a p38-mediated apoptotic pathway. To better understand the relationship between p38 activity and cell survival, we induced apoptosis in two cell lines and examined the ability of insulin or a
specific p38 inhibitor (a pyridinyl imidazole compound PD169316) to
block p38 activity and cell death. In Rat-1 fibroblasts grown in the
presence of serum, p38 activity was undetectable by immune complex
assays, and the number of apoptotic cells was very low (<0.5%). After
the removal of serum for 16 h, p38 activity was markedly elevated,
and apoptosis increased by 14-15-fold. Insulin (50 ng/ml) inhibited
p38 activity by ~70% and blocked apoptosis by at least 80%.
PD169316 also blocked p38 enzyme activity and apoptosis by
approximately 80%. Similar results were obtained in differentiated
PC12 cells that were deprived of nerve growth factor (NGF) for 16 h. In the presence of NGF, p38 activity and the number of apoptotic
cells was very low (~1.0%). After NGF withdrawal, p38 activity was
selectively elevated and apoptosis increased to 15%. Both insulin and
PD169316 markedly blocked the increase in p38 activity and apoptosis.
The MAP kinase kinase inhibitor, PD98059, had no effect on apoptosis in
Rat-1 fibroblasts and only partially blocked apoptosis in PC12 cells.
PD98059 did not influence insulin's ability to block apoptosis,
indicating that the extracellular signal-regulated kinase pathway does
not mediate insulin's survival effects. These data further support the
role of p38 in cellular apoptosis and support the hypothesis that
insulin promotes cell survival, at least in part, by inhibiting the p38
pathway.
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