Interaction of immunoglobulin with actin |
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| Authors: | Marcus Fechheimer John L. Daiss John J. Cebra |
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| Affiliation: | Department of Biology, The Johns Hopkins University, Charles and 34th Streets, Baltimore, MD 21218, U.S.A |
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| Abstract: | ![]()
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. |
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| Keywords: | G-Actin globular actin F-Actin filamentous actin BGG bovine gamma globulin BSA bovine serum albumin PEC peritoneal exudate cells DNP dinitrophenyl DTT dithiothreitol DDA0 di-DNP-diaminooctane SDS sodium dodecyl sulfate ATP adenosine tri-phosphate HEPES |
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