Influence of the subendothelial basement membrane components on fibrin assembly. Evidence for a fibrin binding site on type IV collagen.
Effective repair of a vascular injury depends on establishment of a stable fibrin patch at the injury site. Data presented in this study demonstrate that structural modification of fibrin occurs as a result of fibrin interaction with naturally occurring components of the vascular basement membrane and subendothelial structures. Of the basement membrane components, type IV collagen produces the greatest structural modification, generating thick fibrin fibers; a 3-fold increase in the fiber mass/length ratio occurs when type IV collagen is increased from 0 to 100 ng/ml. Laminin and dermatan sulfate decrease the fibrin fiber mass/length ratio resulting in thinner fibers. However, the overall effect of the basement membrane on fibrin is to increase the fibrin fiber diameter. Electrophoretic light scattering and the binding of type IV collagen by fibrinogen-Sepharose further establish the interaction between type IV collagen and fibrinogen. Incorporation of laminin with type IV collagen onto coated surfaces decreases the ability of type IV collagen to bind fibrinogen. These studies emphasize that the final fibrin structure is influenced by the milieu in which the clot is assembled.
Jones
M
M
Department of Medicine, University of North Carolina, Chapel Hill 27514.
Gabriel
D A
DA
D001485:Basement Membrane / Q000378:metabolism; D002460:Cell Line; D003094:Collagen / Q000378:metabolism*; D003871:Dermatan Sulfate / Q000378:metabolism; D005337:Fibrin / Q000096:biosynthesis* / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism; D007700:Kinetics; D007797:Laminin / Q000378:metabolism; D046911:Macromolecular Substances; D009391:Nephelometry and Turbidimetry; D011485:Protein Binding
D007797:Laminin; D046911:Macromolecular Substances; D003871:Dermatan Sulfate; D005337:Fibrin; D005340:Fibrinogen; D003094:Collagen