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The Journal of Neuroscience, April 1, 2000, 20(7):2567-2574
Role of Glycogen Synthase Kinase-3 in Neuronal Apoptosis
Induced by Trophic Withdrawal
Michal
Hetman1, 2,
Jane
E.
Cavanaugh1, 2,
David
Kimelman3, and
Zhengui
Xia1
1 Toxicology Program in the Department of Environmental
Health, and Graduate Program in Neurobiology and Behavior, Graduate
Program in Molecular and Cell Biology, Departments of
2 Pharmacology and 3 Biochemistry, University
of Washington, Seattle, Washington 98195-7234
Glycogen synthase kinase-3 (GSK3) activity is negatively
regulated by several signal transduction cascades that protect neurons
against apoptosis, including the phosphatidylinositol-3 kinase (PI-3
kinase) pathway. This suggests the interesting possibility that
activation of GSK3 may contribute to neuronal apoptosis. Consequently, we evaluated the role of GSK3 in apoptosis in cultured cortical neurons induced by trophic factor withdrawal or by PI-3 kinase
inhibition. Neurons were subjected to several apoptotic paradigms,
including serum deprivation, serum deprivation combined with exposure
to NMDA receptor antagonists, or treatment with PI-3 kinase
inhibitors. These treatments all led to stimulation of GSK3 activity
in cortical neurons, which preceded the induction of apoptosis.
Expression of an inhibitory GSK3 binding protein or a dominant
interfering form of GSK3 reduced neuronal apoptosis, suggesting that
GSK3 contributes to trophic factor withdrawal-induced apoptosis.
Furthermore, overexpression of GSK3 in neurons increased apoptosis,
indicating that activation of this enzyme is sufficient to trigger
programmed cell death. Although destabilization of -catenin is an
important physiological effect of GSK3 activation, expression of a
mutant -catenin that is not destabilized by GSK3 did not protect
against apoptosis. We conclude that inhibition of GSK3 is one of the
mechanisms by which PI-3 kinase activation protects neurons from
programmed cell death.
Key words:
cortical neurons; glycogen synthase kinase-3; phosphatidylinositol-3 kinase; Akt; -catenin; NMDA; glutamate; brain-derived neurotrophic factor; apoptosis; signal transduction
Copyright © 2000 Society for Neuroscience 0270-6474/00/2072567-08$05.00/0
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A. H. Kim, G. Khursigara, X. Sun, T. F. Franke, and M. V. Chao
Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1
Mol. Cell. Biol.,
February 1, 2001;
21(3):
893 - 901.
[Abstract]
[Full Text]
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