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*
Centocor, Malvern, PA 19355;
Pulmonary and Critical Care Division, University of Pennsylvania Medical Center, Philadelphia, PA 19104;
SmithKline Beecham Labs, King of Prussia, PA 19406;
§
The Blood Research Institute, The Blood Center of Southeastern Wisconsin, Milwaukee, WI 53233; and
¶
Department of Pathology, Stanford University School of Medicine, Palo Alto, CA 94305
Platelet endothelial cell adhesion molecule (PECAM-1), a member of
the Ig superfamily, is found on endothelial cells and neutrophils and
has been shown to be involved in the migration of leukocytes across the
endothelium. Adhesion is mediated, at least in part, through binding
interactions involving its first N-terminal Ig-like domain, but it is
still unclear which sequences in this domain are required for in vivo
function. Therefore, to identify functionally important regions of the
first Ig-like domain of PECAM-1 that are required for the participation
of PECAM-1 in in vivo neutrophil recruitment, a panel of mAbs against
this region of PECAM-1 was generated and characterized in in vitro
adhesion assays and in an in vivo model of cutaneous inflammation. It
was observed that mAbs that disrupted PECAM-1-dependent homophilic
adhesion in an L cell aggregation assay also blocked TNF-
-induced
intradermal accumulation of neutrophils in a transmigration model using
human skin transplanted onto SCID mice. Localization of the epitopes of
these Abs indicated that these function-blocking Abs mapped to specific
regions on either face of domain 1. This suggests that these regions of
the first Ig-like domain may contain or be close to binding sites
involved in PECAM-1-dependent homophilic adhesion, and thus may
represent potential targets for the development of antiinflammatory
reagents.
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