High-affinity binding of bioactive glycosylation-inhibiting factor to antigen-primed T cells and natural killer cells

被引:14
作者
Sugie, K
Nakano, T
Tomura, T
Takakura, K
Mikayama, T
Ishizaka, K
机构
[1] SHIGA UNIV MED SCI,DEPT OBSTET & GYNECOL,OTSU,SHIGA 52021,JAPAN
[2] KIRIN PHARMACEUT LAB,TAKASAKI,GUMMA 37012,JAPAN
关键词
conformational structure; macrophage migration inhibitory factor; suppressor T cells;
D O I
10.1073/pnas.94.10.5278
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
High-affinity binding was demonstrated between suppressor-T-cell-derived bioactive glycosylation-inhibiting factor (GIF) and helper T hybridomas and natural killer cell line cells. Inactive GIF present in cytosol of suppressor T cells and Escherichia coli-derived recombinant human GIF (rhGIF) failed to bind to these cells. However, affinity of rhGIF for the target cells was generated by replacement of Cys-57 in the sequence with Ala or of Asn-106 with Ser or binding of 5-thio-2-nitrobenzoic acid to Cys-60 in the molecule. Such mutations and the chemical modification of rhGIF synergistically increased the affinity of GIF molecules for the target cells. The results indicated that receptors on the target cells recognize conformational structures of bioactive GIF. Equilibrium dissociation constant (K-d) of the specific binding between bioactive rGIF derivatives and high-affinity receptors was 10-100 pM. Receptors for bioactive GIF derivatives were detected on Th1 and Th2 T helper clones and natural killer NK1.1(+) cells in normal spleen but not on naive T or B cells. Neither the inactive rGIF nor bioactive rGIF derivatives bound to macrophage and monocyte lines or induced macrophages for tumor necrosis factor alpha production.
引用
收藏
页码:5278 / 5283
页数:6
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