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Monoclonal antibodies to discrete regions in alpha 2-plasmin inhibitor
J Mimuro, Y Koike, Y Sumi and N Aoki
Three monoclonal antibodies to alpha 2-plasmin inhibitor (alpha 2PI) were
characterized. The first, JTPI-1, was directed against the reative site of
alpha 2PI and inhibited antiplasmin activity by interfering with the
formation of alpha 2PI-plasmin complexes. The avidity of JTPI- 1 to the
preformed alpha 2PI-plasmin complex was markedly lower than that to free
alpha 2PI, which made this antibody useful for measuring the free alpha 2PI
in plasma. The second, JTPI-2, recognized an epitope in the C-terminal
fragment of alpha 2PI (11,000 daltons [11 K]) that was cleaved from alpha
2PI by plasmin upon complex formation but remained noncovalently attached
to the complex. However, binding of JTPI-2 to alpha 2PI was not inhibited
by the C-terminal 26-residue peptide containing the plasminogen-binding
site and had no effect on the function of alpha 2PI. These data suggested
that JTPI-2 recognized an epitope between the C-terminal 26-residue peptide
and the reactive site. The third, JTPI-3, bound the alpha 2PI-plasmin
complex (150 K) as well as alpha 2PI. Binding was inhibited by the
N-terminal 12-residue peptide of alpha 2PI, but factor XIII-catalyzed
cross-linking of alpha 2PI to fibrin was not inhibited by JTPI-3. These
results suggested that the antibody recognized an epitope near the N
terminus. These three monoclonal antibodies were useful for analyzing the
mechanism of interaction between alpha 2PI and plasmin.
Volume 69,
Issue 2,
pp. 446-453,
02/01/1987
Copyright © 1987 by The American Society of Hematology
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