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Vol. 61, Issue 2, 343-351, February 2002
, Src/Proline-Rich Tyrosine Kinase 2, and Epidermal Growth
Factor Receptor trans-Activation
Endocrinology and Reproduction Research Branch, National Institute
of Child Health and Human Development, National Institutes of Health,
Bethesda, Maryland
Agonist activation of endogenous angiotensin II (Ang II)
AT1 receptors expressed in hepatic C9 cells markedly
stimulated inositol phosphate production, phosphorylation of the
proline-rich tyrosine kinase PyK-2, and ERK activation. Ang II caused
activation of protein kinase C 
(PKC) in C9 cells, and its
stimulatory actions on Pyk2 and extracellularly regulated kinase (ERK)
phosphorylation were abolished by PKC depletion and selective
inhibition of PKC by rottlerin, but not by
Ca2+-chelators. These effects, and the similar actions of
the Src kinase inhibitor PP2 indicate the involvement of PKC
and Src kinase in ERK activation. In C9 cells,
phorbol-12-myristate-13-acetate (PMA) caused much greater
phosphorylation of Pyk2 and ERK than the Ca2+ ionophore
ionomycin, and the effects of PMA and Ang II were abolished in
PKC-depleted cells. Ang II increased the association of Pyk2 with Src
and with the epidermal growth factor receptor (EGF-R). EGF caused much
greater tyrosine phosphorylation of the EGF-R than Ang II and PMA. Ang
II-induced activation of ERK, but not Pyk2, was prevented by inhibition
of EGF receptor phosphorylation by AG 1478 and of Src kinase by PP1.
Ang II also increased the association of the adaptor protein Grb2 with
the EGF-R. These findings indicate that Src and Pyk2 act upstream of
the EGF-R and that the majority of Ang II-induced ERK phosphorylation
is dependent on trans-activation of the EGF-R. Ang
II-induced ERK activation in C9 cells is initiated by a
PKC-dependent but Ca2+-independent mechanism and is
mediated by the Src/Pyk2 complex through
trans-activation of the EGF-R.
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