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Blood, Vol. 92 No. 12 (December 15), 1998:
pp. 4721-4729
Structural Studies of Fibrinolysis by Electron Microscopy
Yuri Veklich,
Charles W. Francis,
Janice White, and
John W. Weisel
From the Department of Cell and Developmental Biology, University of
Pennsylvania School of Medicine, Philadelphia, PA; and the Vascular
Medicine Unit, Department of Medicine, University of Rochester School
of Medicine and Dentistry, Rochester, NY.
Fibrin is degraded by the fibrinolytic system in which a plasminogen
activator converts plasminogen to plasmin, a serine protease that
cleaves specific bonds in fibrin leading to solubilization. To
elucidate further the biophysical processes involved in conversion of
insoluble fibers to soluble fragments, fibrin was treated with either
plasmin or the combination of plasminogen and plasminogen activator,
and morphologic changes were observed using scanning electron
microscopy. These changes were correlated with biochemical analysis and
with characterization of released, soluble fragments by transmission
electron microscopy. Initial changes in the fibrin matrix included
creation of many free fiber ends and gaps in the continuity of fibers.
With more extensive digestion, free fiber segments associated
laterally, resulting in formation of thick fiber bundles. Supernatants
of digesting clots, containing soluble derivatives, were negatively
contrasted and examined by transmission electron microscopy. Large,
complex fragments containing portions of multiple fibers were observed,
as were pieces of individual fibers and smaller fragments previously
identified. Some large fragments had sharply defined ends, indicating
that they had been cleaved perpendicularly to the fiber direction.
Other fibers showed splayed ends or a lacy meshwork of surrounding
protofibrils. Longer times generated more small fragments whose
molecular composition could be inferred from their appearance. These
results indicate that fibrinolytic degradation results in larger pieces
than previously identified and that plasmin digestion proceeds locally
by transverse cutting across fibers rather than by progressive cleavage
uniformly around the fiber.
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