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Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in
human thrombi and atherosclerotic lesions
A Bini, J Fenoglio , J Sobel, J Owen, M Fejgl and KL Kaplan
Arterial thrombi and atherosclerotic lesions were analyzed immunochemically
and examined histologically. The extent of in vivo proteolytic cleavage of
the amino-terminal end of fibrinogen by thrombin and plasmin was determined
and quantitated by specific radioimmunoassays. The samples were treated
with cyanogen bromide (CNBr), and the total amount of fibrinogen and
fibrin-derived protein was determined as NDSK, the NH2-terminal disulfide
knot of fibrinogen. Thrombin-releasable fibrinopeptides A and B were used
to quantitate fibrinogen and fibrin I. Previous plasmin cleavage of the B
beta chain was inferred from the amount of B beta 1-42 and B beta 15-42 in
undigested NDSK. The results obtained in both acute and organized thrombi
indicate that approximately 60% of the total protein (as determined by
amino acid analysis) was fibrinogen-derived and that 70% to 80% of the
fibrinogen-derived material was fibrin II. These findings support the
hypothesis that fibrin II as distinct from fibrin I is the predominant
component in a thrombus. In samples from normal and atherosclerotic aortas,
fibrinogen-derived protein comprised less than 10% of the total protein.
Samples from grossly normal aortas contained only fibrinogen and fibrin I.
Fibrinogen concentration decreased and fibrin II concentration increased
with increasing severity of the lesions, suggesting that increased fibrin
II formation is associated with progression of atheromas.
Volume 69,
Issue 4,
pp. 1038-1045,
04/01/1987
Copyright © 1987 by The American Society of Hematology
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