Cloning and characterization of a new intercellular adhesion molecule ICAM-R
| Autor: | Edna S. Dkkinson, Judy K. Tomfta, Rosemay Vazeux, Patricia A. Hoffman, W. Michael Gallatin, Tom St. John, Richard L. Jasman |
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| Rok vydání: | 1992 |
| Předmět: |
Transcription
Genetic Protein Conformation Molecular Sequence Data Integrin CD18 Biology Transfection Cell Line Mice L Cells Cell Adhesion Leukocytes Tumor Cells Cultured Animals Humans Amino Acid Sequence RNA Messenger Cloning Molecular Cell adhesion Peptide sequence Cells Cultured ICAM3 Multidisciplinary ICAM2 Base Sequence Cell adhesion molecule Antibodies Monoclonal DNA Flow Cytometry Intercellular adhesion molecule Molecular biology Models Structural Oligodeoxyribonucleotides biology.protein Endothelium Vascular Cell Adhesion Molecules |
| Zdroj: | Nature. 360:485-488 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/360485a0 |
| Popis: | The human intercellular adhesion molecules ICAM-1, ICAM-2 and their counter-receptors, the beta 2 or leukointegrins, mediate a variety of homotypic and heterotypic leukocyte and endothelial cell-cell adhesions central to immunocompetence. It has been found that cell-cell adhesion which is dependent on expression of the leukocyte function-associated antigen LFA-1 is not always blocked completely by antibodies raised against ICAM-1 and ICAM-2. Other leukointegrin ligands therefore probably exist, such as a glycoprotein of M(r) 124K that binds LFA-1 and has been designated ICAM-3 on the basis of this function. We have molecularly cloned a new member of the ICAM family, ICAM-R, which is related to ICAM-1 and ICAM-2. The complementary DNA encoding ICAM-R is 1,781 base pairs long and the protein has five extracellular immunoglobulin-family type domains. The mature cell-surface form of the ICAM-R protein has an M(r) which varies from 116 to 140K in a cell type-specific fashion. Overall identities in protein sequence with ICAM-1 and ICAM-2 are 48% and 31% respectively, with the degree of similarity varying between individual domains. The high level of expression of ICAM-R on resting leukocytes of all lineages and its lack of expression on either resting or cytokine-activated endothelial cells indicates a pattern of expression distinct from ICAM-1 and ICAM-2. In common with ICAM-1 and ICAM-2, ICAM-R is a ligand for the beta 2-integrin CD11a/LFA-1 (CD18). |
| Databáze: | OpenAIRE |
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