INTERACTION OF IMMUNOGLOBULIN WITH ACTIN

被引：60

作者：

FECHHEIMER, M

DAISS, JL

CEBRA, JJ

机构：

[1] Department of Biology, The Johns Hopkins University, Baltimore, MD 21218

来源：

MOLECULAR IMMUNOLOGY | 1979年 / 16卷 / 11期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

D O I：

10.1016/0161-5890(79)90086-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Actin can form specific, direct associations with immunoglobulin resulting in soluble complexes or cross-linked matrices. This interaction can be detected by four in vitro assays 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 0.1 M KCl 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. © 1979.

引用

页码：881 / 888

页数：8

共 20 条

[1] TRANSMEMBRANE INTERACTIONS AND MECHANISM OF CAPPING OF SURFACE RECEPTORS BY THEIR SPECIFIC LIGANDS [J].