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A monoclonal antibody that recognizes a neo-antigen exposed in the E domain
of fibrin monomer complexed with fibrinogen or its derivatives: its
application to the measurement of soluble fibrin in plasma
G Soe, I Kohno, K Inuzuka, Y Itoh and M Matsuda
Central Research Laboratories, Iatron Laboratories Inc, Chiba, Japan.
Using urea-solubilized human fibrin monomer as an immunogen, we raised in
mice a battery of monoclonal antibodies that reacted with the immunogen but
not with urea-treated or native fibrinogen. Although they all failed to
react with acid-solubilized fibrin monomer (acid-FM) alone, an antibody
designated as IF-43 was found to recognize acid-FM, which was bound with
fibrinogen or its derivatives to form a 1:2 complex of soluble fibrin. The
epitope for this antibody, thus, appears to be exposed most probably by
conformation changes induced in the acid- FM molecule upon formation of the
complex. Because IF-43 was able to recognize fibrin-derived plasmic
fragment E treated with urea but not the thrombin- and urea-treated
amino-terminal disulfide knot of fibrinogen, the presence of the A alpha
(52-78) residue segment seems to be prerequiste for the epitope expression.
The antibody was found to react with soluble fibrin monomer spiked to
normal plasma dose- dependently up to 200 micrograms/mL. By an aggregation
assay using latex beads coated with IF-43, we found that concentrations of
soluble fibrin monomer in plasma derived from patients with thrombotic
diseases were mostly elevated, but not necessarily correlated with those of
the D-dimer, reflecting another aspects of the disease. Furthermore, the
soluble fibrin monomer in plasma derived from patients with thrombotic
diseases was found to be depleted solely of the A peptides, but not the B
peptides, based on its subunit polypeptide compositions lacking the
beta-chain on immunoblotting.
Volume 88,
Issue 6,
pp. 2109-2117,
09/15/1996
Copyright © 1996 by The American Society of Hematology
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