Vanadate stimulates tyrosine phosphorylation of two proteins in Raji human lymphoblastoid cell membranes.
A membrane fraction from Raji human lymphoblastoid cells exhibited tyrosine-specific kinase activity. Vanadate increased tyrosine phosphorylation up to 5-fold; serine and threonine phosphorylation were unchanged. The stimulation was detectable within 15 s at 0 degrees C and at concentrations of vanadate (0.3 and 1.0 microM) present in normal tissues and blood. The tyrosine phosphorylation of two substrates, M1 61 000 and 55 000, was dependent upon vanadate and incorporation into these substrates represented the majority of the vanadate-sensitive tyrosine phosphorylation.
D002051:Burkitt Lymphoma / Q000201:enzymology*; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism* / Q000502:physiology; D011505:Protein-Tyrosine Kinases; D014638:Vanadates; D014639:Vanadium / Q000494:pharmacology*
D008565:Membrane Proteins; D014639:Vanadium; D014638:Vanadates; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases