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Spreading of platelets on fibrin is mediated by the amino terminus of the
beta chain including peptide beta 15-42
M Hamaguchi, LA Bunce, LA Sporn and CW Francis
Department of Medicine, University of Rochester School of Medicine and
Dentistry, NY.
We have investigated the adhesion and spreading of platelets on polymerized
fibrin of varying structure to identify sites that mediate these
interactions. Fibrin was prepared with thrombin to remove both
fibrinopeptide A (FPA) and fibrinopeptide B (FPB) and with reptilase or
Agkistrodon contortrix thrombin-like enzyme (ACTE) to selectively remove
FPA or FPB, respectively. Residual fibrin-bound enzymes were inhibited with
D-phenylalanyl-L-prolyl-L-arginyl chloromethyl ketone (PPACK). Platelet
adhesion was independent of fibrinopeptide cleavage and was equal on fibrin
prepared with each of the three enzymes. In contrast, FPB cleavage
increased spreading as quantitated by fluorescence microscopy of platelets
stained for glycoprotein IIb-IIIa. The 24% +/- 4% spreading on
reptilase-fibrin was significantly less than the 70% +/- 8% on
thrombin-fibrin or 65% +/- 9% on ACTE-fibrin (P < .0005 for both).
Protease III from Crotalus atrox venom was used to specifically cleave
residues B beta 1-42 from fibrinogen to further investigate the role of the
beta chain N-terminus in promoting platelet spreading. After clotting with
thrombin, this fibrin derivative lacked beta 15-42 and supported
significantly less spreading. A monoclonal antibody (MoAb) reactive with
beta 15-21 inhibited spreading on thrombin-fibrin as did peptide beta
15-42, while control MoAbs and peptides had no significant effect. These
results indicate that adhesion and spreading of platelets on fibrin are
mediated by different interactions, and that spreading can be mediated by
FPB cleavage and the amino terminus of the beta chain including residues
beta 15-42.
Volume 81,
Issue 9,
pp. 2348-2356,
05/01/1993
Copyright © 1993 by The American Society of Hematology
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