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(Received for publication, June 20, 1994; and in revised form, January 3, 1995) Neonatal rat cortical astrocytes in primary culture synthesize
and secrete nerve growth factor (NGF) in response to cytokines, growth
factors, and activators of protein kinases. To further implicate a
protein phosphorylation mechanism in the regulation of NGF expression,
astrocytes were treated with okadaic acid and calyculin A, inhibitors
of phosphoprotein phosphatases 1 and 2A. Okadaic acid dramatically
increased both NGF mRNA content (50-fold) and NGF secretion (100-fold)
in astrocytes, while calyculin A, which has a spectrum of phosphatase
inhibitory activity different from okadaic acid, failed to augment NGF
expression. The increased mRNA accumulation was due mainly to an
increase (4-fold) in the half-life of the NGF mRNA following 9 or 24 h
of treatment. Nuclear run-on assays indicated that okadaic acid also
activated NGF gene transcription, which was preceded by an induction of
c-fos and c-jun gene transcription. The induction of
NGF expression by okadaic acid appeared independent from protein kinase
C activity because down-regulating protein kinase C activity failed to
decrease the okadaic acid stimulation. In contrast, interleukin-1
Volume 270,
Number 11,
Issue of March 17, 1995 pp. 5994-5999
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
acted synergistically with okadaic acid to stimulate NGF secretion. The
results indicate that okadaic acid profoundly stimulates NGF expression
in astrocytes mainly by enhancing NGF mRNA stability and suggest
important roles for phosphoprotein phosphatases in regulating NGF
production.
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