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

FEBS Letters

Austin, Kathy S.¹  Shelton Earp, H.¹  Rubin, Richard A.¹  Dy, Ruth C.¹ 

[1] Cell Biology Program, Cancer Research Center, Department of Medicine, 516 Clinical Sciences Building 229H, University of North Carolina School of Medicine, Chapel Hill, NC 27514, USA

关键词: Vanadium;    Lymphocyte;    Protein phosphorylation;    Membrane protein;    Tyrosine-specific kinase;    EGF;    epidermal growth factor;    PDGF;    platelet-derived growth factor;    p-Tyr;    p-Ser;    p-Thr;    phosphotyrosine;    phosphoserine and phosphothreonine;   

DOI  :  10.1016/0014-5793(83)81003-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown