Please use this identifier to cite or link to this item:http://hdl.handle.net/20.500.12105/11922
Title
Endothelial adhesion receptors are recruited to adherent leukocytes by inclusion in preformed tetraspanin nanoplatforms.
Author(s)
Barreiro, Olga CNIC | Zamai, Moreno CNIC | Yanez-Mo, Maria | Tejera, Emilio | Lopez-Romero, Pedro CNIC | Monk, Peter N | Gratton, Enrico | Caiolfa, Valeria R CNIC | Sanchez-Madrid, Francisco CNIC
Date issued
2008-11-03
Citation
J Cell Biol. 2008; 183(3):527-42
Language
Inglés
Document type
journal article
Abstract
VCAM-1 and ICAM-1, receptors for leukocyte integrins, are recruited to cell-cell contact sites on the apical membrane of activated endothelial cells. In this study, we show that this recruitment is independent of ligand engagement, actin cytoskeleton anchorage, and heterodimer formation. Instead, VCAM-1 and ICAM-1 are recruited by inclusion within specialized preformed tetraspanin-enriched microdomains, which act as endothelial adhesive platforms (EAPs). Using advanced analytical fluorescence techniques, we have characterized the diffusion properties at the single-molecule level, nanoscale organization, and specific intradomain molecular interactions of EAPs in living primary endothelial cells. This study provides compelling evidence for the existence of EAPs as physical entities at the plasma membrane, distinct from lipid rafts. Scanning electron microscopy of immunogold-labeled samples treated with a specific tetraspanin-blocking peptide identify nanoclustering of VCAM-1 and ICAM-1 within EAPs as a novel mechanism for supramolecular organization that regulates the leukocyte integrin-binding capacity of both endothelial receptors during extravasation.
MESH
Antigens, CD | Cell Adhesion | Cell Membrane | Endothelium, Vascular | Humans | Integrins | Intercellular Adhesion Molecule-1 | Leukocytes | Membrane Proteins | Microscopy, Confocal | Microscopy, Electron, Scanning | Receptors, Cell Surface | Signal Transduction | Transfection | Tumor Necrosis Factor-alpha | Umbilical Veins | Vascular Cell Adhesion Molecule-1
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DOI
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