Participation of C1q and its receptor in adherence of human diploid fibroblast.

摘要: C1q binds through its collagen-like domain to specific surface receptors of fibroblasts and adhesive elements extracellular matrix including fibronectin, collagens, proteoglycans, laminin. To determine whether participates in fibroblast adhesion, cells serum-free medium were plated on surfaces coated with purified at physiologic ionic strength pH. Surfaces fibronectin or collagen type I served as positive controls, those BSA negative controls. Substratum-adsorbed promoted adhesion a maximum 73% available within 90 min 37 degrees C. Adhesion was concentration dependent, saturable, specific, dependent the molecule. De novo protein synthesis plays role adhesion: pretreatment cycloheximide reduced adherence about 50% Addition exogenous I, soluble mediators did not affect cycloheximide-treated substrate. could be accounted for primarily, although completely, by receptors. Antibodies raised against Raji cell (alpha C1qR Ab) specifically inhibited substrates 60% The binding 24% controls GRGDTP recognition peptide. alpha Ab had an additive effect that 77 80% We conclude from these data aggregated rather than monomeric may natural ligand receptor, biologic function receptor connective tissue adhesion.