Gene interactions and pathways from curated databases and text-mining

◀ Back to MAPK3

MAPK3 — UTP6

Text-mined interactions from Literome

Huwiler et al., Br J Pharmacol 2000 : 3. Time courses reveal that ATP and UTP induce a rapid and transient activation of the p38-MAPK activity with a maximal activation after 5 min of stimulation which declined to control levels over the next 20 min. 4
Tu et al., Br J Pharmacol 2000 (Glioma...) : 3. In response to UTP , both p42 and p44 MAPK were activated in a time- and concentration dependent manner using Western blot analysis with an anti-phospho-p42/p44 MAPK antibody ... Both DNA synthesis and phosphorylation of MAPK in response to UTP were attenuated by tyrosine kinase inhibitors, genistein and herbimycin A, protein kinase C ( PKC ) inhibitors, staurosporine and GF109203X, and removal of Ca ( 2+ ) by addition of BAPTA/AM plus EGTA ... 5. UTP induced [ ( 3 ) H ] -thymidine incorporation and p42/p44 MAPK phosphorylation was completely inhibited by PD98059 ( an inhibitor of MEK1/2 ) ... Furthermore, we showed that overexpression of dominant negative mutants of Ras ( RasN17 ) and Raf ( Raf-301 ) completely suppressed MEK1/2 and p42/p44 MAPK activation induced by ATP and UTP ... UTP mediated MAPK activation was modulated by Ca ( 2+ ), PKC, and tyrosine kinase associated with cell proliferation in cultured C ( 6 ) glioma cells
Santiago-Pérez et al., J Cell Physiol 2001 (MAP Kinase Signaling System) : Accordingly, ERK1/2 phosphorylation induced by UTP was inhibited by the PI3K inhibitors, wortmannin and LY294002, and the c-src inhibitors, radicicol and PP2, but not by inhibitors of protein kinase C ( PKC )
Meshki et al., Am J Physiol Cell Physiol 2004 : ATP and UTP caused activation of p38 MAPK and ERK1/2 in human neutrophils
Morris et al., J Biol Chem 2004 (Cardiomegaly) : In marked contrast, stimulation of G ( q ) -coupled purinergic receptors with UTP caused EGF receptor phosphorylation, ERK1/2 activation, and cellular growth but minimal increases in ANP transcription
Montiel et al., Cell Physiol Biochem 2006 : ATP, 2-meSATP, UTP and UDP cause a rapid and transitory increase in the phosphorylation of MAPK/ERK
Chang et al., Cell Signal 2008 (MAP Kinase Signaling System) : UTP and ATP activated MAPK in a dose- and time dependent manner
Vázquez-Cuevas et al., Reproductive biology and endocrinology : RB&E 2010 (MAP Kinase Signaling System) : It was found that UTP increased MAPK phosphorylation by up to 550 % with an EC50 of 3.34 +/- 0.92 and 1.41 +/- 0.67 microM, for p44 and p42, respectively ; these increases were blocked by suramin
Huwiler et al., Br J Pharmacol 1994 : Activation of mitogen activated protein kinase by both ATP and UTP is dose-dependently attenuated by the P2-receptor antagonist, suramin
Graham et al., Biochem J 1996 : We have investigated the mechanisms that bring about the termination of mitogen activated protein kinase ( MAP kinase ) activation in response to UTP in EAhy 926 endothelial cells
Graham et al., Br J Pharmacol 1996 : Stimulation by the nucleotides, ATP and UTP of mitogen activated protein kinase in EAhy 926 endothelial cells
King et al., Neuroscience 1996 : UTP and 2-methylthioATP stimulated mitogen activated protein kinase to the same extent as ATP, although UTP was less potent than either ATP or 2-methylthioATP
Patel et al., Biochem J 1996 : 2-Methylthio-ATP and UTP , selectively activating P2Y1 and P2Y2 purinoceptors respectively, and ATP, a non-selective agonist at these two receptors, stimulate the tyrosine phosphorylation of both p42mapk and p44mapk , as revealed by Western blots with an antiserum specific for the tyrosine phosphorylated forms of the enzymes