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(Received for publication, July 8, 1996, and in revised form, September 12, 1996)
From the Hubrecht Laboratory, Netherlands Institute for
Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands
In a previous study, we demonstrated that
parathyroid hormone (PTH) inhibits mitogen-activated protein (MAP)
kinase activation in osteosarcoma cells via a protein kinase
A-dependent pathway. Here, we show that PTH can induce a
transient activation of MAP kinase as well. This was observed in both
Chinese hamster ovary R15 cells stably expressing high levels of rat
PTH/PTH-related peptide receptor and parietal yolk sac carcinoma cells
expressing the receptor endogenously. PTH was a strong activator of
adenylate cyclase and phospholipase C in Chinese hamster ovary R15
cells. PTH-induced MAP kinase activation did not depend on activation of Gi, phorbol ester-sensitive protein kinase C, elevated
intracellular calcium levels, or release of G
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3423-3429
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
subunits. It could,
however, be mimicked by addition of forskolin or 8-bromo-cAMP to these cells. Prolonged treatment with forskolin caused sustained protein kinase A activity, whereas MAP kinase activity returned to basal levels. Subsequent treatment with PTH or 8-bromo-cAMP did not result in
MAP kinase activation, whereas phorbol ester- or insulin-induced MAP
kinase activation was unaffected. Finally, expression of a dominant
negative form of Ras (RasAsn-17), which completely blocked
insulin-induced MAP kinase activation, did not affect activation by PTH
or cAMP. In conclusion, PTH regulates MAP kinase activity in a cell
type-specific fashion. The activation of MAP kinase by PTH is mediated
by cAMP and independent of Ras.
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