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- _4 value "In c-MET-overexpressing SCLC cell line NCI-H69, hepatocyte growth factor (HGF) dramatically induced c-MET phosphorylation at phosphoepitopes pY1230/1234/1235 (catalytic tyrosine kinase), pY1003 (juxtamembrane), and also of paxillin at pY31 (CRKL-binding site). We utilised a global proteomics phosphoantibody array approach to identify further c-MET/HGF signal transduction intermediates in SCLC. Strong HGF induction of specific phosphorylation sites in phosphoproteins involved in c-MET/HGF signal transduction was detected, namely adducin-alpha [S724], adducin-gamma [S662], CREB [S133], ERK1 [T185/Y187], ERK1/2 [T202/Y204], ERK2 [T185/Y187], MAPKK (MEK) 1/2 [S221/S225], MAPKK (MEK) 3/6 [S189/S207], RB [S612], RB1 [S780], JNK [T183/Y185], STAT3 [S727], focal adhesion kinase (FAK) [Y576/S722/S910], p38alpha-MAPK [T180/Y182], and AKT1[S473] and [T308]. Conversely, we also identified modest inhibition of phosphorylation by HGF in the following phosphoproteins (Figures 2A and B): PKCa [S657], PKCa/b [T368/641], and PKCd [T505]. Moreover, HGF also inhibited phosphorylation of PKR [T451], which is known to have antiproliferative and pro-apoptotic functions. Lastly, HGF also reduced the threonine and tyrosine phosphorylation of the cell cycle checkpoint regulator CDK1 [T14/Y15]." provenance.
- _4 wasQuotedFrom 17667909 provenance.