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(Received for publication, March 24, 1997, and in revised form, May 19, 1997)
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From the Sustained activation of extracellular
signal-regulated kinase 1/2 (ERK1/2) is critical for initiating
differentiation of the PC12 cell to a sympathetic-like neurone. The
neuropeptide, pituitary adenylyl cyclase-activating peptide (PACAP),
has been demonstrated to cause cells to adopt a neuronal phenotype,
although the mechanism of this activity is unclear. PACAP through its
type I receptor stimulates a biphasic activation of ERK1/2; a >10-fold
increase within 5 min, followed by a >5-fold increase that is
sustained for Department of Medicine and Therapeutics and
the Division of Biochemistry and Molecular Biology, University of
Glasgow, Glasgow G12 8QQ, United Kingdom and the § Cellular
Bioassay Design Group, Lead Discovery Unit, Glaxo-Wellcome,
Medicines Research Centre, Gunnells Wood Road,
Stevenage SG1 2NY, United Kingdom
60 min. An equivalent stimulation is seen in PC12 cells
expressing a dominant negative Ras mutant. However, the
mitogen-activated kinase/ERK kinase 1/2 (MEK1/2) inhibitor PD98059
blocked both PACAP-induced stimulation of ERK1/2 activity and neurite
outgrowth. Thus, the activation signal from the PACAP type I receptor
on the ERK1/2 cascade pathway is received downstream of Ras, either at
Raf or MEK. Down-regulation of protein kinase C or its inhibition by
calphostin C blocked the ability of PACAP to stimulate ERK1/2. We
conclude that activation of PACAP type I receptor activates protein
kinase C, which then activates the ERK1/2 cascade in a Ras-independent
manner at either Raf or MEK1/2.
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