ENHANCED ADHESION OF HUMAN MONONUCLEAR-CELLS TO NONENZYMATICALLY GLYCOSYLATED COLLAGEN-I

Nonenzymatic glycosylation of extracellular matrix components may cont ribute to altered interaction of cells with the matrix. We have examin ed the interaction of mononuclear cells with early glycosylated collag en I. Significantly more cells attached to glycosylated collagen compa red to normal collagen. Radioiodinated glycosylated collagen I specifi cally bound to mononuclear cells in a time and concentration dependent manner with a Kd of 2.45 x 10(-9) M. Maximum binding was observed in the presence of Mn++ ions. The iodinated ligand bound to mononuclear c ell membrane immobilized on nitrocellulose disks and the interaction w as found to be saturable. These results suggested an alteration in the interaction of human blood mononuclear cells with collagen I, when it gets glycosylated non enzymatically and also indicate that early glyc osylated collagen interacts with mononuclear cells through specific, h igh affinity cell surface molecules.