CR1—Cytoskeleton Interactions in Neutrophils
The C3b receptor (CR1) is a polymorphic membrane glycoprotein (Dykman et al., 1983a,b, 1984, 1985; Wong et al., 1983). It is found in a variety of cell types and has several important immunologic functions (see reviews in Fearon, 1985, Schreiber, 1984, and Arnaout and Colten, 1984). For example, aside from mediating attachment of phagocytic cells to opsonized targets, erythrocyte CR1 may function in systemic clearance of complement-containing immune complexes (Cornacoff et al., 1983) or in local inhibition of complement-mediated damage to autologous tissues (Iida and Nussenzweig, 1983). It has been proposed that this function inadvertently plays a roll in the pathogenesis of CR1 deficiency found in patients with systemic lupus erythematosus (Iida et al.,1982). In addition, the human neutrophil CR1 mediates endocytosis of soluble multivalent ligand or soluble C3b-bearing complexes (Fearon et al., 1981; Abrahamson and Fearon, 1983). How this is effected has prompted researchers to investigate the relationship between CR1 and the cytoskeletal apparatus. Among the tools available to accomplish this is nonionic detergent lysis (or extraction) of cells.
KeywordsHuman Neutrophil Phorbol Ester Complement Receptor Phorbol Myristate Acetate Lateral Mobility
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