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|Title:||Fc epsilon RI cross-linking activates a type II phosphatidylinositol 4-kinase in RBL 2H3 cells|
|Keywords:||Mediated Tyrosine Phosphorylation|
Neuronal Calcium Sensor-1
Rat Splenic Lymphocytes
|Publisher:||PERGAMON-ELSEVIER SCIENCE LTD|
|Citation:||MOLECULAR IMMUNOLOGY, 42(12), 1541-1549|
|Abstract:||Crosslinking of Fc epsilon RI on rat basophilic leukemia (RBL 2H3) cells leads to an increase in Phosphatidylinositol 4-kinase activity. This increase in Ptdlns 4-kinase activity is strongly correlated with its tyrosyl phosphorylation state. Characterization of the enzyme activity in anti phosphotyrosine immunoprecipitates suggests it as a type II Ptdlns 4-kinase. Membrane cholesterol depletion studies showed a reduction in type II Ptdlns 4-kinase activity suggesting that lipid rafts play an important role in activation of the enzyme. The enzyme activity was inhibited by resveratrol. In situ inhibition of type II Ptdlns 4-kinase activity showed a reduction in beta-hexosaminidase release upon Fc epsilon RI cross-linking. These studies suggest that a type II Ptdlns 4-kinase is an integral component of Fc epsilon RI mediated signal transduction mechanisms. (c) 2005|
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