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

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
161
Issue
2
Identifiers
DOI: 10.1016/0014-5793(83)81003-5
Keywords
  • Vanadium
  • Lymphocyte
  • Protein Phosphorylation
  • Membrane Protein
  • Tyrosine-Specific Kinase

Abstract

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.

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