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Does the conformation of adsorbed fibrinogen dictate platelet interactions
with artificial surfaces?
JN Lindon, G McManama, L Kushner, EW Merrill and EW Salzman
Platelet activation by polymer surfaces is thought to require preliminary
adsorption of fibrinogen and perhaps changes in fibrinogen conformation. We
measured fibrinogen adsorption by a series of polymers by two methods,
using either 125I-labeled fibrinogen or 125I-labeled antifibrinogen
antibodies, and correlated the results with platelet reactivity (retention
and secretion) in columns of beads coated with the polymers. For polyalkyl
methacrylates with 1 to 4 carbon side chains, platelet reactivity varied
directly with increasing length of the alkyl side chain and with the
quantity of bound fibrinogen recognizable by antifibrinogen antibody but
not with the total quantity of fibrinogen adsorbed. The same pattern of
results was seen with five antibody preparations, including
affinity-purified Fab fragments against the D or E domain of fibrinogen.
Tests of platelet retention and fibrinogen binding to four polyalkyl
acrylates and to three unrelated polymers (polystyrene, polymethyl
methacrylate, and a polyether polyurethane) indicated that platelet
retention correlated positively with both total fibrinogen binding and with
the amount of antibody-recognizable fibrinogen bound. Drugs that block
platelet aggregation, but not adhesion, did not alter the hierarchy of
platelet retention to the polyalkyl methacrylates. These data suggest that,
contrary to previous views, platelet adhesion to artificial surfaces
increases with increasing surface coverage of adsorbed fibrinogen if the
bound fibrinogen maintains a conformation such that its functional domains
remain recognizable by antibody probes.
Volume 68,
Issue 2,
pp. 355-362,
08/01/1986
Copyright © 1986 by The American Society of Hematology
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