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EGF — PLA2G1B

Text-mined interactions from Literome

Croxtall et al., Br J Pharmacol 2000 (MAP Kinase Signaling System) : In the A549 human adenocarcinoma cell line dexamethasone inhibited epidermal growth factor (EGF) stimulated cytosolic PLA(2) ( cPLA(2) ) activation and AA release by blocking the recruitment of Grb2 to the activated EGF receptor (EGF-R) through a glucocorticoid receptor ( GR ) -dependent ( RU486-sensitive ), transcription independent ( actinomycin-insensitive ), mechanism
Spaargaren et al., Biochem J 1992 : Activation of PLA2 by EGF resulted in an enhanced Vmax ... The EGF stimulated PLA2 is Ca ( 2+ ) -dependent, with maximal activity at micromolar concentrations of Ca2+, has a pH optimum at 9, associates with the particulate cell fraction in a Ca ( 2+ ) -dependent fashion, and is selective for arachidonoyl at the sn-2 position ... These data demonstrate the EGF induced activation of a PLA2 , which is similar to a recently cloned high-molecular-mass AA-selective cytosolic PLA2, thus providing a link between EGF-receptor tyrosine kinase activation and AA metabolism
Bonventre et al., J Biol Chem 1990 : This represents a direct demonstration of EGF induced PLA2 activation which is preserved in a cell-free extract ... In summary, EGF results in a stable modification of PLA2 activity in glomerular mesangial cells
Hack et al., Biosci Rep 1990 : We have previously demonstrated phospholipase C (PLC) independent activation of phospholipase A2(PLA2) by epidermal growth factor (EGF) in glomerular mesangial cells in culture
Teitelbaum et al., J Biol Chem 1990 : Studies were performed to examine a potential role for a guanine nucleotide binding protein in epidermal growth factor (EGF) stimulated phospholipase A2 (PLA2) activity ... In contrast to EGF stimulated PLC activity, stimulation of PLA2 by EGF was not susceptible to inhibition by phorbol 12-myristate 13-acetate
Goldberg et al., Biochem J 1990 : We have previously reported that epidermal growth factor (EGF) activates phospholipase A2 (PLA2) independently of phospholipase C (PLC) in renal mesangial cells ... In this study we use NIH 3T3 cell lines transfected with the normal EGF receptor ( HER14 cells ) or with EGF receptor defective in tyrosine kinase activity ( K721A cells ), to determine whether the intrinsic tyrosine kinase activity of the EGF receptor is required for the PLC independent activation of PLA2 ... In HER14 cells, EGF increased PLA2 activity by 226 +/- 30 %, and the tumour promoter phorbol myristate acetate ( PMA ) increased activity by 223 +/- 30 % ... We conclude that the tyrosine kinase activity of the EGF receptor is necessary for the PLC independent stimulation of PLA2 by EGF
Kuroda et al., Nihon Naibunpi Gakkai Zasshi 1988 : These data indicate that an increase of Ca2+ in cytosol is important to PLA2 activation, and also that PLA2 may be activated by PMA, EGF and FBS in thyroid cells
Quigley et al., Am J Physiol 1995 : PLA2 activity, assessed as free arachidonic acid release from proximal tubules in suspension, increased by 18.8 % with 3 nM EGF
Chepenik et al., J Biol Chem 1994 : In vitro nuclear transcription assays showed a parallel increase in the transcription rate of the genes corresponding to CyOx-1 and PLA2c , but not CyOx-2, in response to EGF ... Coordinate regulation of activities of PLA2 and CyOx in response to EGF did not parallel the mitogenic effects of EGF on confluent MEPM cells
Maxwell et al., Biochem J 1993 : We have previously shown that phospholipase A2 (PLA2) activity is rapidly activated by epidermal growth factor (EGF) and phorbol 12-myristate 13-acetate ( PMA ) in renal mesangial cells and other cell systems in a manner that suggests a covalent modification of the PLA2 enzyme ( s )
Goldman et al., Adv Exp Med Biol 1997 : The synergism in PLA2 activation by EGF and TPG or A23187, and the sensitivity of [ 3H ] AA release to N-acetylcysteine (NAC) and dithiothreitol ( DTT ) ( potent reducing agents ) or to DPI ( an inhibitor of FAD dependent oxidases ) lead to the suggestion that ROS formation, elevation of [ Ca2+ ] i and PLA2 activation are causally related