IL‐2‐dependent in vivo and in vitro tyrosine phosphorylation of IL‐2 receptor γ chain

FEBS Letters

Nakamura, Masataka¹  Takeshita, Toshikazu¹  Sugamura, Kazuo¹  Kumaki, Satoru¹  Asao, Hironobu¹ 

[1] Department of Microbiology, Tohoku University School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980, Japan

关键词: Interleukin-2 receptor;    Tyrosine kinase;    IL-2;    interleukin-2;    IL-2R;    interleukin-2 receptor;    FCS;    fetal calf serum;    mAb;    monoclonal antibody;    2D PAGE;    two-dimensional polyacrylamide gel electrophoresis;    PHA;    phytohemagglutinin;    PBL;    peripheral blood leukocyte;   

DOI  :  10.1016/0014-5793(92)80605-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously reported a molecule, p64, which was tentatively named the γ chain, coprecipitable with the β chain of human interleukin-2 receptor (IL-2R). The present study demonstrated that the γ chain, as well as the β chain expressed on IL-2-responsive cells, is phosphorylated on tyrosine residues in an IL-2-dependent manner in vivo and in vitro. The in vivo tyrosine phosphorylation of both chains was similarly induced within 1 min after IL-2 stimulation, and their in vitro tyrosine phosphorylation with the anti-IL-2Rβ antibody-directed immunocomplex was also increased by treatment of cells with IL-2. These results suggest that a tyrosine kinase is associated with the βγ subunit complex, of which activation by IL-2 may result in transduction of intracellular signals.

【 授权许可】

Unknown