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LA Sherman and J Lee
Plasma fibronectin (FN) binds fibrin in vitro by both noncovalent and
covalent bonds and is decreased in DIC. In rabbits, conventionally purified
125I-FN had a complex blood clearance with a late t1/2 of 71 hr. A large
portion was apparently altered, as evinced by rapid clearance and an
intravascular/total body ratio (C1) of 0.28-0.51. 3H- labeled FN, made in
vivo by injection of 3H amino acids, had a t1/2 of 73 hr. Crosstransfusion
of 131I-FN and 3H-FN into a second set of animals gave similar t1/2s and
C1s of 0.74-0.82, indicating the altered 125I-FN was biologically screened
in the first animals. Other animals were given 125I-fibrinogen and
"screened" 131I-FN. Intravenous thrombin (50-60 U/kg/1 hr) caused a 25%-50%
decrease in both 125I-fibrinogen and 131I-FN. Ancrod injection reduced
fibrinogen by greater than 90% but had no effect on 131I-FN. 131I-FN levels
did not change when thrombin was given after ancrod. No cross-linked
FN-fibrinogen alpha-chain was found in the plasma, nor was the
thrombin-induced fall in FN affected by spermidine blockade. These
experiments demonstrate that FN and fibrin bind in vivo during
defibrination and are rapidly cleared from the blood. The abnormal fibrin
resulting from ancrod either does not bind FN in vivo or does so
reversibly.
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