B细胞受体和FcγRIIB1的超聚集激活含Src同源2结构域的蛋白酪氨酸磷酸酶-1。
Superclustering of B cell receptor and Fc gamma RIIB1 activates Src homology 2-containing protein tyrosine phosphatase-1.
作者信息
Sato K, Ochi A
机构信息
The John P. Robarts Research Institute, Department of Microbiology and Immunology, University of Western Ontario, London, Canada.
出版信息
J Immunol. 1998 Sep 15;161(6):2716-22.
Fc gamma RIIB1 (CD32) is a receptor that binds the Fc domain of Ag-complexed IgG. Coaggregation of B cell receptor (BCR) and Fc gamma RIIB1 generates a dominant negative signal that inhibits B cell activation. In Ag-specific Id-positive B cells, the co-cross-linking of BCR and Fc gamma RIIB1 by anti-Id Ab resulted in the association of both Src homology 2-containing protein tyrosine phosphatase (SHP-1) and Src homology 2-containing inositol phosphatase (SHIP) with the Fc gamma RIIB1; however, only SHIP activity was detected. "Superclustering" of the BCR and Fc gamma RIIB1 complex induced by stimulation with anti-Id Ab plus polyvalent Ag synergistically activated SHP-1. The degree of co-cross-linking between BCR and Fc gamma RIIB1 may determine the activation status of SHP-1 and SHIP.
FcγRIIB1（CD32）是一种能与抗原复合物IgG的Fc结构域结合的受体。B细胞受体（BCR）与FcγRIIB1的共聚集产生一种显性负信号，抑制B细胞活化。在抗原特异性Id阳性B细胞中，抗Id抗体使BCR与FcγRIIB1共交联，导致含Src同源2结构域的蛋白酪氨酸磷酸酶（SHP-1）和含Src同源2结构域的肌醇磷酸酶（SHIP）都与FcγRIIB1结合；然而，仅检测到SHIP活性。抗Id抗体加多价抗原刺激诱导的BCR与FcγRIIB1复合物的“超级聚集”协同激活了SHP-1。BCR与FcγRIIB1之间的共交联程度可能决定SHP-1和SHIP的活化状态。
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