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Fibronectin: blood turnover in normal animals and during intravascular coagulation

Journal Article · · Blood; (United States)
OSTI ID:6586835
Plasma fibronectin (FN) binds fibrin in vitro by both noncovalent and covalent bonds and is decreased in DIC. In rabbits, conventionally purified /sup 125/I-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. /sup 3/H-labeled FN, made in vivo by injection of /sup 3/H amino acids, had a t1/2 of 73 hr. Crosstransfusion of /sup 131/I-FN and /sup 3/H-FN into a second set of animals gave similar t1/2s and C1s of 0.74-0.82, indicating the altered /sup 125/-FN was biologically screened in the first animals. Other animals were given /sup 125/I-fibrinogen and screened /sup 131/I-FN. Intravenous thrombin (50-60 U/kg/1 hr) caused a 25%-50% decrease in both /sup 125/I-fibrinogen and /sup 131/I-FN. Ancrod injection reduced fibrinogen by greater than 90% but had no effect on /sup 131/I-FN. /sup 131/I-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.
Research Organization:
Washington University School of Medicine, Division of Laboratory Medicine, St. Louis, MO
OSTI ID:
6586835
Journal Information:
Blood; (United States), Journal Name: Blood; (United States) Vol. 60:3; ISSN BLOOA
Country of Publication:
United States
Language:
English