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LPA — PTK2

Text-mined interactions from Literome

Seufferlein et al., J Biol Chem 1994 : Furthermore, tyrosine phosphorylation of p125FAK induced by LPA was completely prevented when cells were stimulated in the presence of platelet derived growth factor at a concentration ( 30 ng/ml ) that causes disruption of actin stress fibers
Ridley et al., EMBO J 1994 : Genistein also inhibited the Rho dependent clustering of phosphotyrosine containing proteins at focal adhesions, and the increased tyrosine phosphorylation of several proteins including pp125FAK , induced by LPA and bombesin
Saville et al., Biochem J 1994 : In cells where protein kinase C activity was down-regulated or inhibited, ET-1 stimulated tyrosine phosphorylation of pp125fak was reduced to a greater extent than phosphorylation in response to LPA ... In addition, ET-1 stimulated tyrosine phosphorylation of pp80 was decreased by 50-70 % in response to protein kinase C inhibition at both 2 and 60 min whereas LPA stimulated tyrosine phosphorylation of this protein was only reduced at 2 min. Pretreatment with pertussis toxin reduced the tyrosine phosphorylation of pp42 and pp44 forms of mitogen activated protein kinase in response to both ET-1 and LPA but reduced the tyrosine phosphorylation of pp125fak only in response to LPA
McLees et al., Biochem J 1995 : These results are discussed in terms of the pathways regulating both MAP kinase and pp125FAK in response to LPA in the EAhy 926 endothelial cells line
Wang et al., Biochem J 1997 (Second Messenger Systems) : Similarly, PMA also decreased LPA induced tyrosine phosphorylation of p125(FAK) and paxillin without abrogating the response to SPP