Receptor mobility and the binding of cells to lectin-coated fibers.
The ability of cells to bind to nylon fibers coated with lectin molecules interspaced with varying numbers of albumin molecules has been analyzed. The cells used were lymphoma cells, normal lymphocytes, myeloid leukemia cells, and normal and transformed fibroblasts, and the fibers were coated with different densities of concanavalin A or the lectins from soybean or wheat germ. Cells fixed with glutaraldehyde did not bind to lectin-coated fibers. The number of cells bound to fibers could be increased by increasing the density of lectin molecules on the fiber, the density of specific receptors on the cell, or the mobility of the receptors. It is suggested that binding of cells to fibers involves alignment and binding of specific cell surface receptors with lectin molecules immobilized on the fibers, and that this alignment requires short-range rapid lateral mobility (RLM) of the receptors. The titration of cell binding to fibers coated with different densities of lectin and albumin has been used to measure the relative RLM of unoccupied cell surface receptors for the lectin. The results indicate a relationship of RLM to lectin-induced cell-to-cell binding. The RLM or receptors for concanavalin A (Con A) was generally found to be higher than that of receptors for the lectins from wheat germ or soybean. Receptor RLM could be decreased by use of metabolic inhibitors or by lowering the temperature. Receptors for Con A had a lower RLM on normal fibroblasts than on SV40-transformed fibroblasts, and trypsinization of normal fibroblasts increased Con A receptor RLM. Normal lymphocytes, lymphoma cells, and lines of myeloid leukemia cells that can be induced to differentiate had a high receptor RLM, whereas lines of myeloid leukemia cells that could not be induced to differentiate had a low receptor RLM. These results suggest that the RLM of Con A receptors is related to the transformation of fibroblasts and the ability of myeloid leukemia cells to undergo differentiation
D000818:Animals; D001666:Binding Sites, Antibody; D002460:Cell Line; D002462:Cell Membrane / Q000276:immunology; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured / Q000276:immunology*; D003208:Concanavalin A; D004140:Dinitrophenols / Q000494:pharmacology; D005347:Fibroblasts; D037102:Lectins; D007951:Leukemia, Myeloid; D008214:Lymphocytes; D008223:Lymphoma; D051379:Mice; D008954:Models, Biological; D009757:Nylons; D037121:Plant Lectins; D051381:Rats; D012710:Serum Albumin, Bovine; D013539:Simian virus 40; D013025:Glycine max; D013696:Temperature; D014908:Triticum / Q000276:immunology
D004140:Dinitrophenols; D037102:Lectins; D009757:Nylons; D037121:Plant Lectins; D003208:Concanavalin A; D012710:Serum Albumin, Bovine