Vanadate stimulates tyrosine phosphorylation of two proteins in Raji human lymphoblastoid cell membranes

Abstract
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°C and at concentrations of vanadate (0.3 and 1.0 μM) present in normal tissues and blood. The tyrosine phosphorylation of two substrates, M 1 61 000 and 55 000, was dependent upon vanadate and incorporation into these substrates represented the majority of the vanadate-sensitive tyrosine phosphorylation.