JAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cells

Author:

Moog-Lutz Christel1,Cavé-Riant Florence1,Guibal Florence C.1,Breau Marie A.1,Di Gioia Yolande1,Couraud Pierre Olivier1,Cayre Yvon E.1,Bourdoulous Sandrine1,Lutz Pierre G.1

Affiliation:

1. From Hôpital Robert Debré, Institut National de la Santé et de la Recherche Médicale (INSERM) Unité 417; and Institut Cochin, INSERM Unité 567, Centre National de la Recherche Scientifique (CNRS) UMR8104, Université Paris V, Paris, France.

Abstract

AbstractRetinoic acid induces clinical remission in acute promyelocytic leukemia (APL) by triggering differentiation of leukemia promyelocytes. Here, we have characterized a gene encoding a member of the immunoglobulin superfamily, among novel retinoic acid–induced genes identified in APL cells. This protein, which was named JAML (junctional adhesion molecule–like), contains 2 extracellular immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic tail. JAML mRNA is expressed in hematopoietic tissues and is prominently expressed in granulocytes. The fact that JAML protein is localized at the cell plasma membrane in the areas of cell-cell contacts, whereas it is not detected at free cell borders, suggests that JAML is engaged in homophilic interactions. Furthermore, a conserved dimerization motif among JAM members was shown to be important for JAML localization at the cell membrane. Finally, exogenous expression of JAML in myeloid leukemia cells resulted in enhanced cell adhesion to endothelial cells. Altogether, our results point to JAML as a novel member of the JAM family expressed on leukocytes with a possible role in leukocyte transmigration.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

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