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(Received for publication, September 4, 1996)
From the Many G protein-coupled receptors
(e.g. that of angiotensin II) activate phospholipase C
Volume 271, Number 47,
Issue of November 22, 1996
pp. 29993-29998
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
CORRELATION WITH c-Jun N-TERMINAL KINASE BUT NOT
MITOGEN-ACTIVATED PROTEIN KINASE ACTIVATION
,
,
,
,
,
,
,
and
Lineberger Comprehensive Center, Departments
of Medicine and Pharmacology, University of North Carolina at Chapel
Hill School of Medicine, Chapel Hill, North Carolina 27599, the
§ Protein and Peptide Group, European Molecular Biology
Laboratory, Heidelberg D-69012, Germany, and ¶ Glaxo Wellcome
Research and Development,
Research Triangle Park, North Carolina 27709
,
initially increasing intracellular calcium and activating protein
kinase C. In the WB and GN4 rat liver epithelial cell lines,
agonist-induced calcium signals also stimulate tyrosine phosphorylation
and subsequently increase the activity of c-Jun N-terminal kinase
(JNK). We have now purified the major calcium-dependent
tyrosine kinase (CADTK), and by peptide and nucleic acid sequencing
identified it as a rat homologue of human PYK2. CADTK/PYK2 is most
closely related to p125FAK and both enzymes are expressed
in WB and GN4 cells. Angiotensin II, which only slightly increases
p125FAK tyrosine phosphorylation in GN4 cells,
substantially increased CADTK tyrosine autophosphorylation and kinase
activity. Agonists for other G protein-coupled receptors
(e.g. LPA), or those increasing intracellular calcium
(thapsigargin), also stimulated CADTK. In comparing the two rat liver
cell lines, GN4 cells exhibited ~ 5-fold greater angiotensin II-
and thapsigargin-dependent CADTK activation than WB cells.
Although maximal JNK activation by stress-dependent pathways (e.g. UV and anisomycin) was equivalent in the two
cell lines, calcium-dependent JNK activation was 5-fold
greater in GN4, correlating with CADTK activation. In contrast to JNK,
the thapsigargin-dependent calcium signal did not activate
mitogen-activated protein kinase and Ang II-dependent
mitogen-activated protein kinase activation was not correlated with
CADTK activation. Finally, while some
stress-dependent activators of the JNK pathway (NaCl and
sorbitol) stimulated CADTK, others (anisomycin, UV, and TNF
) did
not. In summary, cells expressing CADTK/PYK2 appear to have two
alternative JNK activation pathways: one stress-activated and the other
calcium-dependent.
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