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JAM-2, a novel immunoglobulin superfamily molecule, expressed by endothelial and lymphatic cells

Duncan, L.
Ballestrem, Christoph
Published in Journal of Biological Chemistry. 2001, vol. 276, no. 4, p. 2733-2741
Abstract Cell-cell contacts are essential for morphogenesis and tissue function and play a vital role in mediating endothelial cohesion within the vascular system during vessel growth and organization. We identified a novel junctional adhesion molecule, named JAM-2, by a selective RNA display method, which allowed identification of transcripts encoding immunoglobulin superfamily molecules regulated during coculture of endothelial cells with tumor cells. The JAM-2 transcript is highly expressed during embryogenesis and is detected in lymph node and Peyer's patches RNA of adult mice. Accordingly, antibodies specific for JAM-2 stain high endothelial venules and lymphatic vessels in lymphoid organs, and vascular structures in the kidney. Using real time video microscopy, we show that JAM-2 is localized within minutes to the newly formed cell-cell contact. The role of the protein in the sealing of cell-cell contact is further suggested by the reduced paracellular permeability of cell monolayer transfected with JAM-2 cDNA, and by the localization of JAM-2 to tight junctional complexes of polarized cells. Taken together, our results suggest that JAM-2 is a novel vascular molecule, which participates in interendothelial junctional complexes.
Keywords Amino Acid SequenceAnimalsBase SequenceCell Adhesion Molecules/genetics/ isolation & purificationCell CompartmentationCell PolarityEndothelium, Lymphatic/ chemistry/ultrastructureEndothelium, Vascular/ chemistry/ultrastructureImmunoglobulins/genetics/ isolation & purificationKidney/blood supplyMembrane Proteins/genetics/ isolation & purificationMiceMolecular Sequence DataReceptors, Cell SurfaceSequence Homology, Amino AcidTight Junctions/ chemistry/ultrastructureTissue Distribution
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PMID: 11053409
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