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Proteolysis of platelet glycoprotein Ib by plasmin is facilitated by
plasmin lysine-binding regions
B Adelman, AD Michelson, J Greenberg and RI Handin
We have characterized the effects of plasmin on glycoprotein Ib (GpIb), a
platelet membrane receptor for von Willebrand factor (vWF), and on
glycocalicin, a fragment of the alpha chain of GpIb that contains the
vWF-binding region. The addition of 4.5 X 10(-7) mol/L plasmin to washed
platelets caused a time-dependent decrease in ristocetin- induced,
vWF-dependent platelet agglutination. epsilon-Aminocaproic acid (EACA)
inhibited plasmin release of glycocalicin-related antigen from washed
platelets and preserved vWF-dependent platelet agglutination, thus
indicating that the lysine-binding sites on plasmin facilitated its
degradation of GpIb. To demonstrate a direct interaction between plasmin
and the vWF-binding region of GpIb we incubated purified glycocalicin with
plasmin. Plasmin degraded the glycocalicin into two small carbohydrate-poor
peptides and into a larger carbohydrate-rich fragment. EACA was able to
inhibit plasmin- mediated degradation of glycocalicin in a
concentration-dependent fashion. These studies indicated that plasmin
degradation of GpIb was due to a direct interaction between plasmin and
GpIb and that this effect was mediated by the lysine-binding region of the
plasmin molecule.
Volume 68,
Issue 6,
pp. 1280-1284,
12/01/1986
Copyright © 1986 by The American Society of Hematology
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