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Blood Research Institute, Blood Center of Southeastern Wisconsin, Milwaukee, WI 53233
Platelet-endothelial cell adhesion molecule-1 (PECAM-1) is a
130-kDa transmembrane glycoprotein expressed by endothelial cells,
platelets, monocytes, neutrophils, and certain T cell subsets. The
PECAM-1 extracellular domain has six Ig-homology domains that share
sequence similarity with cellular adhesion molecules. The PECAM-1
cytoplasmic domain contains an immunoreceptor tyrosine-based inhibitory
motif (ITIM) that, when appropriately engaged, becomes phosphorylated
on tyrosine residues, creating docking sites for nontransmembrane, Src
homology 2 domain-bearing protein tyrosine phosphatase (SHP)-1 and
SHP-2. The purpose of the present study was to determine whether
PECAM-1 inhibits protein tyrosine kinase (PTK)-dependent signal
transduction mediated by the immunoreceptor tyrosine-based activation
motif-containing TCR. Jurkat cells, which coexpress PECAM-1 and the
TCR/CD3 complex, were INDO-1AM-labeled and then incubated with
anti-CD3
mAbs, anti-PECAM-1 mAbs, or both, and goat
anti-mouse IgG was used to cross-link surface-bound mAbs. Calcium
mobilization induced by CD3 cross-linking was found to be attenuated by
coligation of PECAM-1 in a dose-dependent manner. PECAM-1-mediated
inhibition of TCR signaling was attributable, at least in part, to
inhibition of release of calcium from intracellular stores. These data
provide evidence that PECAM-1 can dampen signals transduced by
ITAM-containing receptors and support inclusion of PECAM-1 within the
family of ITIM-containing inhibitors of PTK-dependent signal
transduction.
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