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Studies on the ultrastructure of fibrin lacking fibrinopeptide B (beta-
fibrin)
MW Mosesson, JP DiOrio, MF Muller, JR Shainoff, KR Siebenlist, DL Amrani, GA Homandberg, J Soria, C Soria and M Samama
Release of fibrinopeptide B from fibrinogen by copperhead venom
procoagulant enzyme results in a form of fibrin (beta-fibrin) with weaker
self-aggregation characteristics than the normal product (alpha
beta-fibrin) produced by release of fibrinopeptides A (FPA) and B (FPB) by
thrombin. We investigated the ultrastructure of these two types of fibrin
as well as that of beta-fibrin prepared from fibrinogen Metz (A alpha 16
Arg----Cys), a homozygous dysfibrinogenemic mutant that does not release
FPA. At 14 degrees C and physiologic solvent conditions (0.15 mol/L of
NaCl, 0.015 mol/L of Tris buffer pH 7.4), the turbidity (350 nm) of rapidly
polymerizing alpha beta-fibrin (thrombin 1 to 2 U/mL) plateaued in less
than 6 min and formed a "coarse" matrix consisting of anastomosing fiber
bundles (mean diameter 92 nm). More slowly polymerizing alpha beta-fibrin
(thrombin 0.01 and 0.001 U/mL) surpassed this turbidity after greater than
or equal to 60 minutes and concomitantly developed a network of thicker
fiber bundles (mean diameters 118 and 186 nm, respectively). Such matrices
also contained networks of highly branched, twisting, "fine" fibrils (fiber
diameters 7 to 30 nm) that are usually characteristic of matrices formed at
high ionic strength and pH. Slowly polymerizing beta-fibrin, like slowly
polymerizing alpha beta-fibrin, displayed considerable quantities of fine
matrix in addition to an underlying thick cable network (mean fiber
diameter 135 nm), whereas rapidly polymerizing beta-fibrin monomer was
comprised almost exclusively of wide, poorly anastomosed, striated cables
(mean diameter 212 nm). Metz beta-fibrin clots were more fragile than those
of normal beta-fibrin and were comprised almost entirely of a fine network.
Metz fibrin could be induced, however, to form thick fiber bundles (mean
diameter 76 nm) in the presence of albumin at a concentration (500 mumol/L)
in the physiologic range and resembled a Metz plasma fibrin clot in that
regard. The diminished capacity of Metz beta-fibrin to form thick fiber
bundles may be due to impaired use or occupancy of a polymerization site
exposed by FPB release. Our results indicate that twisting fibrils are an
inherent structural feature of all forms of assembling fibrin, and suggest
that mature beta-fibrin or alpha beta-fibrin clots develop from networks of
thin fibrils that have the ability to coalesce to form thicker fiber
bundles.
Volume 69,
Issue 4,
pp. 1073-1081,
04/01/1987
Copyright © 1987 by The American Society of Hematology
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