Abstract
Fodrin, a protein composed of 2 polypeptides with MW of 250,000 and 240,000, is concentrated in the cortical cytoplasm of neurons, and moves down the axons by the process of axonal transport. Immunofluorescence techniques were used to determine whether fodrin antigens also move in nonneuronal cells when cell surface ligands are induced to redistribute by crosslinking them. A redistribution of fodrin antigens occurred in the following instances: when [mouse fibroblasts] 3T3 cells were incubated with concanavalin A [Con A] and anti-Con A, surface Con A receptors formed aggregates and fodrin antigens formed corresponding intracellular aggregates; when B lymphocytes were incubated with anti-Ig, the surface Ig formed caps and fodrin antigens formed intracellular subcaps; when T lymphocytes were treated with anti-H-2 followed by a secondary antibody, the H-2 antigen formed caps and fodrin formed corresponding subcaps. Fodrin antigens can move within nonneuronal cells as well as in axons, and their organization can be regulated by interaction between surface proteins and environmental stimuli. Fodrin, together with other proteins that form subcaps in lymphocytes (e.g., actin, myosin and .alpha.-actinin), may be a component of the cellular machinery responsible for the capping process. Whether the similarities between the movements of fodrin in lymphocyte capping and axonal transport indicate that certain aspects of these 2 processes are related is considered.

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