Induction of phosphotyrosine in the gap junction protein, connexin43

FEBS Letters

Husøy, Trine¹  Vikhamar, Gunnhild¹  Mikalsen, Svein-Ole¹  Sanner, Tore¹ 

[1] Laboratory for Environmental and Occupational Cancer, Institute for Cancer Research, The Norwegian Radium Hospital, N-0310 Oslo, Norway

关键词: Protein-tyrosine phosphatase inhibitor;    Hydrogen peroxide;    Pervanadate;    Permolybdate;    Phosphotyrosine;    Connexin;    GJIC;    gap junctional intercellular communication;    Cx43;    connexin43;    SHE;    Syrian hamster embryo;    PTPase;    protein-tyrosine phosphatase;    Vanadate;    orthovanadate;    NP;    P1;    P2;    the non-phosphorylated and the major phosphorylated forms of Cx43;   

DOI  :  10.1016/S0014-5793(96)01489-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein-tyrosine phosphatase inhibitors pervanadate, permolybdate, H₂O₂, and to a much lesser extent vanadate, increased the amount of cellular phosphotyrosine and induced tyrosine phosphorylation of connexin43 (Cx43) in early passage hamster embryo fibroblasts. The presence of phosphotyrosine in Cx43 immunoprecipitates from pervanadate-treated cells was shown by a phosphotyrosine-specific antibody and a phosphotyrosine-specific phosphatase. Pervanadate-induced Cx43 tyrosine phosphorylation was further verified by phosphoamino acid analysis, while no phosphotyrosine was present in control cells. This is the first observation of tyrosine phosphorylation of connexins in normal cells.

【 授权许可】

Unknown