ヒト及びマウスインターロイキン2レセプター複合体の免疫化学的解析
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Normal activated T cells and Adult T cell leukemia cells express two classes of interleukin 2 receptors (IL-2R), high and low affinity IL-2R. The growth signal seems to be delivered by IL-2R bound to the high affinity, but not the low affinity IL-2R. In this communication, we present a series of experiments we have conducted to find whether the high affinity IL-2R has an associated molecule. Cell surface antigens expressed on human and mouse cells were chemically cross-linked by DTSSP. Immunoprecipitation study with anti-Tac antibody demonstrated that a 75,000 dalton associated molecule as well as a 110,000 dalton molecule were detected on cells that express high affinity IL-2R, but not on cells that express only low affinity IL-2R. In order to confirm that the 75kd associated molecule plays an important role in the transmembrane signal transduction, cDNA coding for human p55 was transfected into mouse L cells and T cells. L cells only expressed p55 while IL-2R did not promote any growth. In contrast, mouse T cell expressed both p55 and the 75kd associated molecules. The proliferation of those T cells was inhibited by exogeneous recombinant IL-2, thus indicating that the 75kd associated molecule plays a crucial role in IL-2 mediated signal transduction. Furthermore, to discover which is the important part of p55 in its functional association with 75kd associated molecule, we have obtained cDNA encoding a chimeric receptor consisting of the extracellar portion of Tac antigen and the transmembrane as well as the cytoplasmic portion of the human insulin receptor. The cDNA was tronsfected into mouse T cells. These T cells expressed high and low affinity IL-2R, mediated IL-2 specific incibition of cell growth, and expressed associated molecules, suggesting that the extracellar region of p55 is important for the association between p55 and 75kd associated molecule. ?Recent studies suggest the presence of second IL-2 binding protein (β chain) which is present on the surface of cells that express high affinity IL-2R. In this communication we present a series of experiments we have also conducted to discover if the high affinity IL-2R has a β chain and relationship between the β chain and associated molecules. Chemical cross-linking study of 125I-labeled IL-2 demonstrated that the 75,000-80,000 dalton as well as 55,000 dalton (α chain) molecule was detected on the cells that expressed high affinity IL-2R, but not on the cells that expressed only low affinity IL-2R, and the Tac antibody blocks the binding of 125I-labeled IL-2 to p55 as well as p75 (β chain). These results suggest the possibility that 75kd associated molecule and p75 (β chain) are the same molecule and that this molecule plays an important role in signal transduction
- 札幌医科大学の論文
- 1988-06-01
札幌医科大学 | 論文
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