Redistribution of intermediate filaments during capping of lymphocyte surface molecules

Abstract

Intermediate filaments (IF) constitute a major cytoplasmic filamentous network of higher eukaryotic cells that is distinct from actin and myosin microfilaments or microtubules. Although structurally similar, these filaments are formed by chemically and antigenically different proteins. Vimentin is the major IF polypeptide of mesenchymal cells and cultured non-mesenchymal cell lines¹. Recently, we have characterized a monoclonal IgM antibody from a patient with Waldenström's macroglobulinaemia which is directed against vimentin². Using this monoclonal antibody, we have shown by direct immunofluorescence that intermediate filaments of human B and T lymphocytes consist of vimentin. In cells exposed to colcemid, the intermediate filaments retracted into a juxta-nuclear aggregate (‘coil’) characteristic of vimentin filaments. As most components of the cytoskeleton, especially actin³ and myosin⁴, have been implicated in the capping phenomenon, we investigated the effect of capping of either β₂-micro globulin or membrane immunoglobulins on the organization of the intermediate filament network. We report that capping of these surface molecules induced the redistribution of vimentin just beneath the cap. When colcemid-treated cells were allowed to cap, the location of the cap always coincided with the coil, suggesting that the anchorage point of intermediate filaments is situated within the uropod.