INTERACTION OF IMMUNOGLOBULIN WITH ACTIN
INTERACTION OF IMMUNOGLOBULIN WITH ACTIN
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DOI：
10.1016/0161-5890(79)90086-5
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发表时间：
1979-01-01
影响因子：
3.6
通讯作者：
CEBRA, JJ
中科院分区：
文献类型：
--
作者：
FECHHEIMER, M;DAISS, JL;CEBRA, JJ
肌动蛋白可以与免疫球蛋白形成特异性的直接缔合，从而产生可溶性复合物或交联基质。这种相互作用可以通过使用纯化组分的四种体外测定来检测：（1）肌动蛋白增强豚鼠IgG 2的亲细胞活性;（2）在低离子强度的溶液中，肌动蛋白和IgG 2共沉淀：（3）在0.1MKCl中存在可溶性复合物，当存在IgG 1，IgG 2，或IgM;（4）免疫球蛋白（IgG 1、IgG 2、BGG）β：增加F-肌动蛋白溶液的粘度，推测是通过交联F-肌动蛋白丝。这些数据表明，细胞骨架蛋白与细胞表面受体的直接相互作用是可能的。
Actin can form specific, direct associations with immunoglobulin resulting in soluble complexes or cross-linked matrices. This interaction can be detected by fourin vitroassays using purified components: (1) actin enhances the cytophilic activity of guinea pig IgG2; (2) in solutions of low ionic strength, actin and IgG2 co-precipitate: (3) soluble complexes exist in 0.1MKCl as revealed by the displacement of actin from its expected sedimentation pattern in a gradient of sucrose when in the presence of IgG 1, IgG2, or IgM; (4) immunoglobulin (IgG1, IgG2, BGG)‡: increases the viscosity of F-actin solutions, presumably by crosslinking F-actin filaments. These data suggest that direct interaction of a cytoskeletal protein with a cell surface receptor is possible.