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Vol. 285, Issue 1, 325-334, April 1998
Endocrine Research Group, Department of Pharmacology & Therapeutics
and Department of Medicine, The University of Calgary Faculty of
Medicine, Calgary, Alberta, Canada T2N 4N1
Using a guinea pig gastric longitudinal smooth muscle preparation, we
have compared the contractile signaling pathways triggered by the
thrombin receptor-activating peptide, TFLLR-NH2 (TF) and by
epidermal growth factor-urogastrone (EGF). In addition to inhibitors of
tyrosine kinase [tyrphostin 47/AG213, genistein and the src-selective inhibitor CP118,556/PP1], cyclooxygenase (indomethacin, INDO) and
diacylglycerol lipase (U57, 908), we also used the signal pathway probe
inhibitors of mitogen-activated protein-kinase-kinase (MEK:PD98059),
phosphatidylinositol 3'-kinase [PI3K: Wortmannin (WM) and LY294002],
protein kinase C [PKC: GF109203X (GF)], and of the EGF-receptor
kinase (PD153035). We found that in addition to the inhibition of both
TF and EGF-stimulated contractions by the inhibitors of tyrosine
kinase, cyclooxygenase and diacylglycerol lipase, the actions of TF and
EGF were also attenuated by PD98059, WM/LY294002 and GF. However,
PD153035 blocked only EGF-triggered contractions. The contractile
actions of both TF and EGF were dependent on extracellular calcium. In
contrast, the contractile action of arachidonic acid, via a presumed
cyclooxygenase product that mediated the contractions caused by both TF
and EGF, was not blocked by any of the signal pathway probe inhibitors.
The contractile actions of both TF and EGF were accompanied by
increases in tissue phosphotyrosyl proteins and an increase in tissue
c-src kinase activity. We conclude that protease-activated receptor no.
1- (thrombin receptor) mediated contractions in the logitudial muscle,
like EGF receptor-activated responses, require the influx of
extracellular calcium and use parallel signal pathways upstream of the
cyclooxygenase step, involving MEK, PI3K, kinase C and possibly
cellular src. The TF-induced response did not involve trans-activation
of the EGF receptor kinase; but the converse (i.e.,
trans-activation of protease-activated receptor no. 1 (thrombin receptor) by the EGF receptor kinase) could not be ruled out.
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