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J Biol Chem, Vol. 275, Issue 19, 14182-14189, May 12, 2000
From the Department of Biomedical Sciences, College of Veterinary
Medicine, Cornell University, Ithaca, New York 14853
Receptors coupled to heterotrimeric G proteins
are linked to activation of mitogen-activated protein kinases (MAPKs)
via receptor- and cell-specific mechanisms. We have demonstrated
recently that gonadotropin-releasing hormone (GnRH) receptor occupancy
results in activation of extracellular signal-regulated kinase (ERK)
through a mechanism requiring calcium influx through L-type calcium
channels in
Divergent Signaling Pathways Requiring Discrete Calcium Signals
Mediate Concurrent Activation of Two Mitogen-activated Protein Kinases
by Gonadotropin-releasing Hormone*
T3-1 cells and primary rat gonadotropes. Further studies
were undertaken to explore the signaling mechanisms by which the GnRH receptor is coupled to activation of another member of the MAPK family,
c-Jun N-terminal kinase (JNK). GnRH induces activation of the JNK
cascade in a dose-, time-, and receptor-dependent manner in
clonal T3-1 cells and primary rat pituitary gonadotrophs. Coexpression of dominant negative Cdc42 and kinase-defective
p21-activated kinase 1 and MAPK kinase 7 with JNK and ERK indicated
that specific activation of JNK by GnRH appears to involve these
signaling molecules. Unlike ERK activation, GnRH-stimulated JNK
activity does not require activation of protein kinase C and is not
blocked after chelation of extracellular calcium with EGTA.
GnRH-induced JNK activity was reduced after treatment with the
intracellular calcium chelator BAPTA-AM
(1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid acetoxymethyl ester), whereas activation of ERK was not affected. Chelation of intracellular calcium also reduced GnRH-induced activation of JNK in rat pituitary cells in primary culture. GnRH-induced induction and activation of the JNK target c-Jun was inhibited after
chelation of intracellular calcium, whereas induction of c-Fos, a known
target of ERK, was unaffected. Therefore, although activation of ERK by
GnRH requires a specific influx of calcium through L-type calcium
channels, JNK activation is independent of extracellular calcium but
sensitive to chelation of intracellular calcium. Our results
provide novel evidence that GnRH activates two MAPK superfamily members
via strikingly divergent signaling pathways with differential
sensitivity to activation of protein kinase C and mobilization of
discrete pools of calcium.
*
This work was supported by National Institutes of Health
Postdoctoral Fellowship MH11105 (to J. M. M.) and National Institutes of Health Grant HD34722 (to M. S. R.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biomedical
Sciences, T6-008a Veterinary Research Tower, Cornell University, Ithaca, NY 14853. Tel.: 607-253-3469; Fax: 607-253-3851; E-mail: msr14@cornell.edu.
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