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Vanadate stimulates tyrosine phosphorylation of two proteins in Raji human lymphoblastoid cell membranes
Author(s) -
Shelton Earp H.,
Rubin Richard A.,
Austin Kathy S.,
Dy Ruth C.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)81003-5
Subject(s) - vanadate , phosphorylation , tyrosine phosphorylation , tyrosine , serine , lymphoblast , biochemistry , raji cell , threonine , biology , chemistry , microbiology and biotechnology , cell culture , cell , genetics
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.