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Peritoneal macrophages elicited in various ways exhibited marked wheat germ agglutinin (WGA)-dependent cytolytic activity against MM46 cells [nearly 100% lysis at effector to target ratio (E/T) = 40], while macrophage cell lines J774.1 and WEHI-3 cells showed less activity (-25% at E/T = 0.63-2.5) and no cytolysis (E/T = 40), respectively. Studies on the kinetics of WGA-binding showed that peritoneal macrophages had an association constant (Ka) of 0.09-0.18 X 10(6) M-1 and the number of their binding sites (N) was 2-7.7 X 10(7)/cell, while the Ka and N values of J774.1 and WEHI-3 cells were 1.2 X 10(6) M-1 and 4.1 X 10(7)/cell and 0.6 X 10(6) M-1 and 5.4 X 10(7)/cell, respectively. On the other hand, cytolytic target MM46 cells showed values of 0.27 X 10(6) M-1 and 1.8 X 10(8)/cell. Lower affinities and moderate numbers of binding sites coincided with the efficient WGA-dependent cytolytic activities of the effector cells. The surface of peritoneal macrophages and J774.1 and MM46 cells was iodinated, the cells lysed, the lysates fractionated on a WGA-Sepharose column and the WGA-binding surface-glycoproteins in GlcNAc-specific fractions of the eluate were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Peritoneal macrophages gave three major bands of 153 kilo dalton (kDa), 140 and 90 kDa proteins, whereas J774.1 and MM46 cells both gave 6 bands of very similar molecular weights and intensities that were quite unlike those of peritoneal macrophages.(ABSTRACT TRUNCATED AT 250 WORDS)

Glycoprotein receptors to wheat germ agglutinin on the surface of murine macrophages.