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Blood, 1 September 2001, Vol. 98, No. 5, pp. 1440-1447
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Regulation of P-selectin binding to the neutrophil P-selectin
counter-receptor P-selectin glycoprotein ligand-1 by neutrophil
elastase and cathepsin G
Elizabeth E. Gardiner,
Mariagrazia De Luca,
Tracy McNally,
Alan D. Michelson,
Robert K. Andrews, and
Michael C. Berndt
From the Hazel and Pip Appel Vascular Biology
Laboratory, Baker Medical Research Institute, Melbourne, Australia; and
the Center for Platelet Function Studies, University of Massachusetts
Medical School, Worcester, MA.
In the inflammatory response, leukocyte rolling before adhesion and
transmigration through the blood vessel wall is mediated by specific
cell surface adhesion receptors. Neutrophil rolling involves the
interaction of P-selectin expressed on activated endothelium and its
counter-receptor on neutrophils, P-selectin glycoprotein ligand-1
(PSGL-1). Here, it is reported that P-selectin binding to neutrophils
is lost under conditions that cause the release of proteinases from
neutrophil primary granules. Treatment of neutrophils with the purified
neutrophil granule proteinases, cathepsin G and elastase, rapidly
abolished their capacity to bind P-selectin. This inactivation
corresponded to loss of the N-terminal domain of PSGL-1, as assessed by
Western blot analysis. A loss of intact PSGL-1 protein from the
surfaces of neutrophils after the induction of degranulation was also
detected by Western blot analysis. Cathepsin G initially cleaved near
the PSGL-1 N-terminus, whereas neutrophil elastase predominantly
cleaved at a more C-terminal site within the protein mucin core.
Consistent with this, cathepsin G cleaved a synthetic peptide based on
the PSGL-1 N-terminus between Tyr-7/Leu-8. Under conditions producing
neutrophil degranulation in incubations containing mixtures of
platelets and neutrophils, the loss of PSGL-1, but not P-selectin, from
platelet-neutrophil lysates was detected. Cathepsin G- or neutrophil
elastase-mediated PSGL-1 proteolysis may constitute a potential
autocrine mechanism for down-regulation of neutrophil adhesion to
P-selectin.
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