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Blood, Vol. 93 No. 3 (February 1), 1999:
pp. 876-885
Platelet/Polymorphonuclear Leukocyte Interaction: P-Selectin Triggers
Protein-Tyrosine Phosphorylation-Dependent CD11b/CD18
Adhesion: Role of PSGL-1 as a Signaling Molecule
Virgilio Evangelista,
Stefano Manarini,
Rita Sideri,
Serenella Rotondo,
Nicola Martelli,
Antonio Piccoli,
Licia Totani,
Paola Piccardoni,
Dietmar Vestweber,
Giovanni de Gaetano, and
Chiara Cerletti
From the Istituto di Ricerche Farmacologiche Mario Negri, Unit of
Biology of Cell Interactions, "Giulio Bizzozero" Laboratory of
Platelet and Leucocyte Pharmacology; Laboratory of Tumor and Vascular
Cell Biology, Department of Vascular Medicine and Pharmacology,
Consorzio Mario Negri Sud, Santa Maria Imbaro, Italy; and Institute of
Cell Biology, ZMBE, University of Muenster, Muenster, Germany.
Polymorphonuclear leukocyte (PMN) adhesion to activated platelets is
important for the recruitment of PMN at sites of vascular damage and
thrombus formation. We have recently shown that binding of activated
platelets to PMN in mixed cell suspensions under shear involves
P-selectin and the activated  2-integrin CD11b/CD18. Integrin activation required signaling mechanisms that were sensitive to tyrosine kinase inhibitors.1 Here we show that mixing
activated, paraformaldehyde (PFA)-fixed platelets with PMNs under shear
conditions leads to rapid and fully reversible tyrosine phosphorylation
of a prominent protein of 110 kD (P~110). Phosphorylation was both
Ca2+ and Mg2+ dependent and was blocked by
antibodies against P-selectin or CD11b/CD18, suggesting that both
adhesion molecules need to engage with their respective ligands to
trigger phosphorylation of P~110. The inhibition of P~110
phosphorylation by tyrosine kinase inhibitors correlates with the
inhibition of platelet/PMN aggregation. Similar effects were observed
when platelets were substituted by P-selectin-transfected Chinese
hamster ovary (CHO-P) cells or when PMN were stimulated with
P-selectin-IgG fusion protein. CHO-P/PMN mixed-cell aggregation and
P-selectin-IgG-triggered PMN/PMN aggregation as well as P~110 phosphorylation were all blocked by antibodies against P-selectin or
CD18. In each case PMN adhesion was sensitive to the tyrosine kinase
inhibitor genistein. The antibody PL-1 against P-selectin glycoprotein
ligand-1 (PSGL-1) blocked platelet/PMN aggregation, indicating that
PSGL-1 was the major tethering ligand for P-selectin in this
experimental system. Moreover, engagement of PSGL-1 with a nonadhesion
blocking antibody triggered 2-integrin-dependent genistein-sensitive aggregation as well as tyrosine phosphorylation in
PMN. This study shows that binding of P-selectin to PSGL-1 triggers
tyrosine kinase-dependent mechanisms that lead to CD11b/CD18 activation in PMN. The availability of the 2-integrin to
engage with its ligands on the neighboring cells is necessary for the tyrosine phosphorylation of P~110.
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