Human C1q induces eosinophil migration.

Eosinophils (Eo) play a significant role in allergic inflammation and the host's immunity to parasitic infections. Although the presence of C1q-binding cell surface molecule(s) (C1q-R) on Eo had been previously implicated by the ability of C1q to augment IgG-dependent, Eo-mediated killing of schistosomula, little is known about the structure or the function of this receptor. The present studies were therefore undertaken to immunochemically demonstrate and to examine the biology of Eo C1q-R. Eo were purified to homogeneity (>90%) and viability (>98%) from hypereosinophilic donors by Percoll density gradient. Western blot analysis using antibodies to cC1q-R and gC1q-R showed distinct bands corresponding to cC1q-R (60 kDa) and gC1q-R (33 kDa) when immunoblotted with their respective antibodies. The Eo C1q-R was tested for its ability to induce chemokinesis and/or chemotaxis as assessed by the modified Boyden microchamber assay utilizing 5-micrometer-pore polycarbonate membranes and using C1q, cC1q, or gC1q (10 micrograms/ml) as agonists. The known chemotactic factors C5a and RANTES (10(-8)M) were used as positive controls. The results showed that at this concentration, cC1q was most efficient in its ability to induce Eo migration (20 +/- SEM 12, n = 4) followed by C1q (107 +/- SEM 7, n=7) and gC1q (77 +/- SEM 10, n = 10). When checkerboard analysis was performed, the data indicated that the observed phenomenon was likely to be due largely to chemokinesis. As expected, C5a (145 +/- SEM 15, n = 7) and RANTES (145 +/- SEM 43, n = 7) were both chemotactic. Furthermore, incubation of Eo with 50 micrograms of either C1q, gC1q, or cC1q (1 hr, 37 degrees C) did not cause release of eosinophil cationic protein as measured by RIA, nor did it enhance the expression of CD11b or CD29 as assessed by FACS analysis. The data presented in this paper show that Eo express both cC1q-R and gC1q-R and may participate in Eo function by providing a primary signal for locomotion.