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J. Biol. Chem., Vol. 277, Issue 36, 32985-32991, September 6, 2002

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Fibroblast Growth Factor 1 Regulates Signaling via the Glycogen Synthase Kinase-3 Pathway
IMPLICATIONS FOR NEUROPROTECTION^*

Makoto Hashimoto, Yutaka Sagara, Dianne Langford^§, Ian P. Everall^¶, Margaret Mallory, Analisa Everson, Murat Digicaylioglu, and Eliezer Masliah^§**

From the Departments of  Neurosciences and ^§ Pathology, University of California San Diego, La Jolla, California 92093-0624, the ^¶ Section of Experimental Neuropathology and Psychiatry, Institute of Psychiatry, London SE5 8AF, United Kingdom, and  The Burnham Institute, Center for Neuroscience and Aging, La Jolla, California 92037

We hypothesize that in neurodegenerative disorders such as Alzheimer's disease and human immunodeficiency virus encephalitis the neuroprotective activity of fibroblast growth factor 1 (FGF1) against several neurotoxic agents might involve regulation of glycogen synthase kinase-3 (GSK3), a pathway important in determining cell fate. In primary rat neuronal and HT22 cells, FGF1 promoted a time-dependent inactivation of GSK3 by phosphorylation at serine 9. Blocking FGF1 receptors with heparinase reduced this effect. The effects of FGF1 on GSK3 were dependent on phosphatidylinositol 3-kinase (PI3K)-protein kinase B (Akt) because inhibitors of this pathway or infection with dominant negative Akt adenovirus blocked inactivation. Furthermore, treatment of neuronal cells with FGF1 resulted in ERK-independent Akt phosphorylation and -catenin translocation into the nucleus. On the other hand, infection with wild-type GSK3 recombinant adenovirus-associated virus increased activity of GSK3 and cell death, both of which were reduced by FGF1 treatment. Moreover, FGF1 protection against glutamate toxicity was dependent on GSK3 inactivation by the PI3K-Akt but was independent of ERK. Taken together these results suggest that neuroprotective effects of FGF1 might involve inactivation of GSK3 by a pathway involving activation of the PI3K-Akt cascades.

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