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J Biol Chem, Vol. 274, Issue 42, 29796-29804, October 15, 1999
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From the Departments of The hypothalamic decapeptide
gonadotropin-releasing hormone stimulates mobilization of two discrete
pools of calcium in clonal ( Biomedical Sciences and
§ Molecular Medicine, College of Veterinary Medicine,
Cornell University, Ithaca, New York 14853
T3-1) and primary pituitary
gonadotropes. A multidisciplinary approach was implemented to
investigate the effects of discrete calcium fluctuations on the
signaling pathways linking the gonadotropin-releasing hormone receptor
to activation of mitogen-activated protein kinases and immediate early
genes. Blockade of calcium influx through nifedipine-sensitive
voltage-gated calcium channels reduced buserelin-induced activation of
extracellular signal-regulated kinase (ERK) and c-Fos while activation
of c-Jun N-terminal kinase and c-Jun was unaffected. Inhibition of
buserelin-stimulated ERK activity by nifedipine was also observed in
rat pituitary cells in primary culture. Direct activation of T3-1
cell L-type calcium channels with the agonist Bay-K 8644 resulted in
phosphorylation of ERK and induction of c-Fos. However, simple
voltage-induced channel activation did not produce a sufficient calcium
signal, since depolarization with 35 mM KCl failed to
induce activation of ERK. Depletion of intracellular calcium stores
with thapsigargin did not affect buserelin-induced ERK activation. An
inhibitor of protein kinase C decreased calcium influx through
nifedipine-sensitive calcium channels and phosphorylation of ERK
induced by buserelin. Pharmacological inhibition of protein kinase C
did not block Bay-K 8644-induced ERK activation. These observations
suggest that calcium influx through L-type channels is required for
GnRH-induced activation of ERK and c-Fos and that the influence of
calcium lies downstream of protein kinase C.
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