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Interaction of Fibronectin
with Blood Coagulation Proteins
Fibronectin was first identified as a contaminant in crude preparations
of fibrinogen, the main blood clotting protein
[529].
The two proteins associate reversibly but only in the cold where they tend
to coprecipitate especially in the presence of heparin. Fibronectin is
covalently incorporated into fibrin clots through the transglutaminase
action of coagulation factor
XIII [ref].
The presence of Fn in the clot matrix affects its mechanical properties
and may have important implications for the ensuing process of wound healing
and clot dissolution. Fibrin matrices that contain Fn are much better substrates
for fibroblast
adhesion and spreading than are those lacking Fn [ref].
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