A role of secreted glycosaminoglycans in cell-substratum adhesion.

An adhesion-deficient variant, designated M3A, was derived from the anchorage-dependent L6 skeletal muscle myoblast line (Schubert, D., and La Corbiere, M. (1980) J. Biol. Chem. 255, 11557-11563). To investigate the defect in the M3A variant, adhesion to various substrata was studied. M3A adhered rapidly to substrate-attached material (SAM) prepared from L6 cultures and serum, but adhered slowly to SAM derived from M3A itself. The role of collagen and fibronectin in the adhesion of M3A cells to L6- and M3A-derived SAMs was ruled out, but several experiments suggested that glycosaminoglycans play a rate-limiting role in the adhesion process. The adhesive interaction of the M3A cells with the different substrata is specific with respect to the glycosaminoglycans involved, since the type and concentration of purified glycosaminoglycans required to inhibit the interaction is unique to each surface. An alteration in glycosaminoglycan synthesis by M3A cells may account for the difference in the adhesive properties of SAM derived from L6 and from the M3A variant.