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Blood, Vol. 94 No. 11 (December 1), 1999:
pp. 3800-3805
Regulation of c-Jun-NH2 Terminal Kinase and Extracellular-Signal
Regulated Kinase in Human Platelets
Franck Bugaud,
Florence Nadal-Wollbold,
Sylviane Lévy-Toledano,
Jean-Philippe Rosa, and
Marijke Bryckaert
From U348 INSERM, IFR Circulation Lariboisière, Hôpital
Lariboisière, Paris, France.
Platelets are an interesting model for studying the relationship
betwen adhesion and mitogen-activated protein (MAP) kinase activation.
We have recently shown that in platelets, ERK2 was activated by
thrombin and downregulated by  IIb 3
integrin engagement. Here we focused our attention on the c-Jun
NH2-terminal kinases (JNKs) and their activation in conditions of
platelet aggregation. We found that JNK1 was present in human platelets
and was activated after thrombin induction. JNK1 phosphorylation was
detected with low concentrations of thrombin (0.02 U/mL) and after 1 minute of thrombin-induced platelet aggregation. JNK1 activation was increased (fivefold) when fibrinogen binding to
IIb3 integrin was inhibited by the
Arg-Gly-Asp-Ser (RGDS) peptide or
(Fab')2 fragments of a monoclonal antibody specific
for IIb3, demonstrating that, like ERK2,
IIb3 integrin engagement negatively
regulates JNK1 activation. Comparison of JNK1 activation by thrombin in stirred and unstirred platelets in the presence of RGDS peptide showed
a positive regulation by stirring itself, independently of
IIb3 integrin engagement, which was
confirmed in a thrombasthenic patient lacking platelet
IIb3. The same positive regulation by
stirring was found for ERK2. These results suggest that MAP kinases
(JNK1 and ERK2) are activated positively by thrombin and stirring. In
conclusion, we found that JNK1 is present in platelets and can be
activated after thrombin induction. Moreover, this is the first report
showing that two different MAP kinases (ERK2 and JNK1) are regulated
negatively by IIb3 engagement and
positively by mechanical forces in platelets.
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