Defective thrombolysis due to collagen incorporation in fibrin clots.
The migration of fibroblasts into a clot may be responsible at least in part, for its organization, thus leading to a defective thrombolysis. We have shown that collagen incorporated in a fibrin clot induces a dramatic decrease in fibrinolysis. Despite the fact that plasminogen binds to collagen, tissue plasminogen activator induced plasminogen activation in the presence of fibrin is only slightly decreased by the presence of collagen. This rather suggests that collagen induces a modification in clot structure, by rendering fibrin less accessible to fibrinolytic enzyme.
Mirshahi
M
M
Laboratoire d'Immunohématologie, C.H.U. Lariboisière, Paris, France.
Soria
J
J
Lu
H
H
Soria
C
C
Samama
M
M
Caen
J P
JP
D000818:Animals; D003094:Collagen / Q000378:metabolism*; D005337:Fibrin / Q000378:metabolism*; D005342:Fibrinolysis; D010958:Plasminogen / Q000378:metabolism; D011137:Polystyrenes; D011817:Rabbits; D013927:Thrombosis / Q000378:metabolism*; D010959:Tissue Plasminogen Activator / Q000378:metabolism
D011137:Polystyrenes; D005337:Fibrin; D010958:Plasminogen; D003094:Collagen; D010959:Tissue Plasminogen Activator