Inhibition of Neutrophil Chemotaxis by a Monoclonal Antibody (TM316)

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Abstract
A monoclonal antibody, TM316, IgM, was raised against the human monocytoid leukaemia cell line THP‐1, and was shown to inhibit polymorphonuclear leucocyte (PMN) chemotaxis. The molecular weight (MW) of the protein on the PMN membrane with which TM316 bound was about 78,000. TM316 inhibited the chemotactic response of human PMN induced by at least three kinds of chemotactic factors (activated serum, N‐formyl‐l‐methionyl‐l‐leucyl‐l‐phenylalanine (FMLP), and a lymphocyte‐derived chemotactic factor (LDCF)) to the same extent. The extent of inhibition of chemotaxis by TM316 was strongly correlated with the quantity of cellular surface antigen recognized by TM316, when a cell sorter was used for analysis. TM316 did not alter the number of Fc or complement receptors of PMN, nor did it affect luminol‐enhanced chemiluminescence(CL), lysosomal enzyme release, adherence, or superoxide anion generation by PMN. TM316 seemed to recognize a common surface antigen which was necessary only for the process of chemotaxis.