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Blood, 1 January 2002, Vol. 99, No. 1, pp. 137-144
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Platelet endothelial cell adhesion molecule-1 signaling inhibits
the activation of human platelets
Milenko Cicmil,
Joanne M. Thomas,
Mireille Leduc,
Cassian Bon, and
Jonathan M. Gibbins
From the School of Animal and Microbial Sciences,
University of Reading, United Kingdom; and Institute Pasteur, Paris,
France.
Platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) is a
130-kd transmembrane glycoprotein and a member of the growing family of
receptors with immunoreceptor tyrosine-based inhibitory motifs (ITIMs).
PECAM-1 is expressed on platelets, certain T cells, monocytes,
neutrophils, and vascular endothelial cells and is involved in a range
of cellular processes, though the role of PECAM-1 in platelets is
unclear. Cross-linking of PECAM-1 results in phosphorylation of the
ITIM allowing the recruitment of signaling proteins that bind by way of
Src-homology domain 2 interactions. Proteins that have been implicated
in the negative regulation of cellular activation by ITIM-bearing
receptors include the tyrosine phosphatases SHP-1 and SHP-2. Tyrosine
phosphorylation of immunoreceptor tyrosine-based activatory motif
(ITAM)-bearing receptors such as the collagen receptor GPVI-Fc
receptor  -chain complex on platelets leads to activation. Increasing
evidence suggests that ITIM- and ITAM-containing receptors may act
antagonistically when expressed on the same cell. In this study it is
demonstrated that cross-linking PECAM-1 inhibits the aggregation and
secretion of platelets in response to collagen and the GPVI-selective
agonist convulxin. In these experiments thrombin-mediated platelet
aggregation and secretion were also reduced, albeit to a lesser degree
than for collagen, suggesting that PECAM-1 function may not be
restricted to the inhibition of ITAM-containing receptor pathways.
PECAM-1 activation also inhibited platelet protein tyrosine
phosphorylation stimulated by convulxin and thrombin; this was
accompanied by inhibition of the mobilization of calcium from
intracellular stores. These data suggest that PECAM-1 may play a role
in the regulation of platelet function in vivo.
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