Investigation of the attachment of bovine corneal endothelial cells to collagens and other components of the subendothelium. Role of fibronectin.
Bovine corneal endothelial cells adhered equally well to a variety of collagens (types I, III, IV and V) consistent with a role for fibronectin in this process. They did not exhibit a preferential binding to collagen type IV--as might be anticipated if laminin were to play a significant role in their adhesion. Inhibition studies with anti-fibronectin antibodies demonstrated the importance of endogenous fibronectin in the mediation of attachment. Consistent with this, binding did not appear to require the presence of exogenous protein, since cells bound to collagens equally well in the presence or absence of added fibronectin and binding was not stimulated by pretreatment of collagens with this protein.
D000818:Animals; D002417:Cattle; D002448:Cell Adhesion; D003094:Collagen / Q000378:metabolism*; D003315:Cornea / Q000166:cytology; D003513:Cycloheximide / Q000494:pharmacology; D004727:Endothelium / Q000166:cytology* / Q000378:metabolism; D005353:Fibronectins / Q000502:physiology*; D006023:Glycoproteins / Q000502:physiology*; D007797:Laminin; D014357:Trypsin / Q000494:pharmacology
D005353:Fibronectins; D006023:Glycoproteins; D007797:Laminin; D003094:Collagen; D003513:Cycloheximide; D014357:Trypsin