The Journal of Experimental Medicine
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Published 2 September 2002. doi:10.1084/jem.20020267
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© Rockefeller University Press, 0022-1007/2002/9/679/ $5.00
The Journal of Experimental Medicine, Volume 196, Number 5, September 2, 2002 679-691

The Junctional Adhesion Molecule 3 (JAM-3) on Human Platelets is a Counterreceptor for the Leukocyte Integrin Mac-1

Sentot Santoso1, Ulrich J.H. Sachs1, Hartmut Kroll1, Monica Linder2, Andreas Ruf4, Klaus T. Preissner2 and Triantafyllos Chavakis2,3

1 Institute for Clinical Immunology and Transfusion Medicine, Internal Medicine, Justus-Liebig-University, D-35385 Giessen, Germany
2 Institute for Biochemistry, Internal Medicine, Justus-Liebig-University, D-35385 Giessen, Germany
3 3rd Department, Internal Medicine, Justus-Liebig-University, D-35385 Giessen, Germany
4 Institute for Clinical Laboratory Diagnostics, Klinikum Karlsruhe, 76133 Karlsruhe, Germany

Address correspondence to Sentot Santoso, Institute for Clinical Immunology and Transfusion Medicine, Justus Liebig University Giessen, Langhansstrasse 7, D-35385 Giessen, Germany. Phone: 49-641-99-41518; Fax: 49-641-99-41529. E-mail: sentot.santoso{at}immunologie.med.uni-giessen.de

The recently described junctional adhesion molecules (JAMs) in man and mice are involved in homotypic and heterotypic intercellular interactions. Here, a third member of this family, human JAM-3, was identified and described as a novel counterreceptor on platelets for the leukocyte ß2-integrin Mac-1 ({alpha}Mß2, CD11b/CD18). With the help of two monoclonal antibodies, Gi11 and Gi13, against a 43-kD surface glycoprotein on human platelets, a full-length cDNA encoding JAM-3 was identified. JAM-3 is a type I transmembrane glycoprotein containing two Ig-like domains. Although JAM-3 did not undergo homophilic interactions, myelo-monocytic cells adhered to immobilized JAM-3 or to JAM-3–transfected cells. This heterophilic interaction was specifically attributed to a direct interaction of JAM-3 with the ß2-integrin Mac-1 and to a lower extent with p150.95 ({alpha}Xß2, CD11c/CD18) but not with LFA-1 ({alpha}Lß2, CD11a/CD18) or with ß1-integrins. These results were corroborated by analysis of K562 erythroleukemic cells transfected with different heterodimeric ß2-integrins and by using purified proteins. Moreover, purified JAM-3 or antibodies against JAM-3 blocked the platelet-neutrophil interaction, indicating that platelet JAM-3 serves as a counterreceptor for Mac-1 mediating leukocyte–platelet interactions. JAM-3 thereby provides a novel molecular target for antagonizing interactions between vascular cells that promote inflammatory vascular pathologies such as in atherothrombosis.

Key Words: monoclonal antibody • adhesion molecule • integrins • neutrophils • athero- thrombosis


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