Relationship between regeneration of cell surface glycoproteins in trypsin-treated chick embryo fibroblasts and cell adhesion to the substratum

1978 ◽  
Vol 34 (6) ◽  
pp. 736-737 ◽  
Author(s):  
M. Vernay ◽  
M. Cornic ◽  
M. Aubery ◽  
R. Bourrillon
Keyword(s):  
Cell Adhesion ◽  
Chick Embryo ◽  
Cell Surface ◽  
Cell Surface Glycoproteins ◽  
Embryo Fibroblasts ◽  
Surface Glycoproteins

Recognition of collagen by fibroblasts through cell surface glycoproteins reactive with Phaseolus vulgaris agglutinin

1992 ◽  
Vol 101 (3) ◽  
pp. 625-633
Author(s):  
H. Asaga ◽  
K. Yoshizato
Keyword(s):  
Phaseolus Vulgaris ◽  
Cell Surface ◽  
Ricinus Communis ◽  
Specific Binding ◽  
Collagen Gel ◽  
Collagen Fibrils ◽  
Pokeweed Mitogen ◽  
Collagen Gel Contraction ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

The role of glycochains of cell surface glycoproteins in the cell to collagen interaction was examined by studying the effect of lectins on the fibroblast-mediated collagen gel contraction. Lectins of Phaseolus vulgaris agglutinin (PHA), concanavalin A (ConA), lentil seed agglutinin (LCA), pea agglutinin (PSA), Ricinus communis agglutinin-60 (RCA), and wheat germ agglutinin (WGA) dose-dependently inhibited gel contraction, while lectins of mushroom agglutinin (ABA), peanut agglutinin (PNA), pokeweed mitogen (PWM), and soybean agglutinin (SBA) did not. Of these lectins, PHA seemed to be worthy of further analysis, because PHA, but not other lectins, inhibited spreading of fibroblasts on collagen fibrils but not on plastic or gelatin, suggesting that cell-surface glycoproteins responsive to the lectin are involved in the specific binding of fibroblasts to native collagen fibrils. The inhibitory effect of PHA-E4, an isolectin of PHA, was more intense than that of PHA-L4, another isolectin of PHA. The collagen gel contraction was also inhibited by tunicamycin and monensin in a concentration-dependent and reversible manner. These results strongly suggest that PHA-E4-reactive glycoproteins of the fibroblast surface play an important role in cell to collagen binding during the gel contraction. Five membrane proteins including beta 1 subunits of the integrin family were obtained by affinity chromatography with PHA-E4.

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