[Effect of substances that disrupt cell adhesion to the substrate on the glycoprotein spectrum of normal fibroblasts in culture].

Alterations of glycoproteins pattern of normal mouse and chick embryo fibroblasts, caused by chemicals impairing cell-substrate adhesion were studied in culture. The chemicals used were proteases (trysin, pronase and papain), EDTA and urea. Using sodium dodecyl sulfat polyacrylamide gel electrophoresis, it was shown that mouse fibroblasts contained four major high-molecular mass glycoproteins that were removed from cells when the adhesion was impaired. Their apparent molecular masses were estimated to be 268 000 (GP-268), 260 000 (GP-260), 211 000 (GP-211) and 196 000 (GP-196). Each glycoprotein proved to be senitive only to one treatment: GP-268 - to very low doses of proteases (1--10 microgram/ml, 10 min), GP-260 - to long treatment with urea (1 M, 2h), GP-211 and GP-196 - to cell rounding and detachment from the substrate caused by long treatment with EDTA (200 microgram/ml, 30 min). In contrast to mouse cells, chick fibroblasts contained only one major high-molecular mass glycoprotein with an apparent molecular mass 266 000 (GP-266) sensitive to all the treatments tested, but to a different degree. The role of glycoproteins studied in the process of cell-substrate adhesion as well as the dependence of certain glycoproteins (GP-211 and GP-196) on the cell shape is discussed.