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Does apolipoprotein(a) heterogeneity influence lipoprotein(a) effects on
fibrinolysis?
L Hervio, MJ Chapman, J Thillet, S Loyau and E Angles-Cano
Institut National de la Sante et de la Recherche Medicale, INSERM U. 143,
Hopital de Bicetre, Paris, France.
High plasma levels of lipoprotein(a) [Lp(a)] are considered to be an
independent risk factor for premature cardiovascular disease and are
inversely associated with apolipoprotein(a) [apo(a)] isoform sizes. The
contribution of apo(a) polymorphism to the inhibition of fibrinolysis, a
mechanism that may favor thrombus development, was therefore evaluated by
measuring the ability of Lp(a) particles of distinct apo(a) isoform content
to compete with plasminogen for fibrin binding during plasminogen
activation by fibrin-bound tissue-type plasminogen activator. The rate of
plasmin generation was most efficiently inhibited by an isoform with a
molecular weight (M(r)) of approximately 540 Kd. An isoform with M(r)
approximately 590 Kd produced a less pronounced effect, whereas the isoform
with M(r) approximately 610 Kd failed to inhibit plasminogen activation.
These effects were directly proportional to the amount of Lp(a) bound to
the carboxy-terminal lysine residues of degraded fibrin. The relative
affinity of the binding (kd range, 16 to 180 nmol/L) reflected the ability
of individual Lp(a) isoforms to inhibit the binding of plasminogen (kd, 600
nmol/L). The question of the influence of kringle sequence variability on
the binding to fibrin was not addressed by the present work. These data
suggest that apo(a) isoform types with high affinity for fibrin may
influence the ability of Lp(a) to interfere with fibrinolysis and
contribute thereby to the association of elevated levels of Lp(a) with
atherosclerotic and thrombotic risks.
Volume 82,
Issue 2,
pp. 392-397,
07/15/1993
Copyright © 1993 by The American Society of Hematology
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