Chemotaxis of mitogen-activated human lymphocytes and the effects of membrane-active enzymes.

Following incubation with polyclonal activators such as PHA or concanavalin A, human peripheral blood lymphocytes show directional migration towards chemotactic factors such as endotoxin-activated plasma, casein or denatured proteins. This migration is inhibited by treatment of the cells with phospholipase C and sphingomyelinase C, but little affected by proteases or glycosidases. In addition, these lymphocytes migrate towards PHA and other lymphocyte activators when these reagents are used as chemoattractants at concentrations well below their mitogenic doses. They also migrate towards staphylococcal protein A. Migration towards PHA and protein A is reduced by pretreating the lymphocytes with proteases but not with phospholipase C. These results suggest two independent membrane interactions which initiate lymphocyte chemotaxis, one acting directly via the lipid bilayer, the other involving the binding of ligands to membrane proteins.