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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Nguyen, T. Bowen, B. R. Lasky, L. A. |
| Description | Author Affiliation: Bowen BR ( Department of Cardiovascular Research, Genentech, Inc., South San Francisco, California 94080.) |
| Abstract | Lymphocyte trafficking is a fundamental aspect of the immune system that allows B and T lymphocytes with diverse antigen recognition specificities to be exposed to various antigenic stimuli in spatially distinct regions of an organism. A lymphocyte adhesion molecule that is involved with this trafficking phenomenon has been termed the homing receptor. Previous work (Lasky, L., T. Yednock, M. Singer, D. Dowbenko, C. Fennie, H. Rodriguez, T. Nguyen, S. Stachel, and S. Rosen. 1989. Cell. 56:1045-1055) has characterized a cDNA clone encoding a murine homing receptor that is involved in trafficking of lymphocytes to peripheral lymph nodes. This molecule was found to contain a number of protein motifs, the most intriguing of which was a carbohydrate binding domain, or lectin, that is apparently involved in the adhesive interaction between murine lymphocytes and peripheral lymph node endothelium. In this study, we have used the murine cDNA clone to isolate a human homologue of this peripheral lymph node-specific adhesion molecule. The human receptor was found to be highly homologous to the murine receptor in overall sequence, but showed no sequence similarity to another surface protein that may be involved with human lymphocyte homing, the Hermes glycoprotein. The extracellular region of the human receptor contained an NH2 terminally located carbohydrate binding domain followed by an EGF-like domain and a domain containing two repeats of a complement binding motif. Transient cell transfection assays using the human receptor cDNA showed that it encoded a surface glycoprotein that cross reacted with a polyclonal antibody directed against the murine peripheral lymph node homing receptor. Interestingly, the human receptor showed a high degree of sequence homology to another human cell adhesion glycoprotein, the endothelial cell adhesion molecule ELAM. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 109 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1989-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Adhesion Membrane Glycoproteins Physiology Receptors, Immunologic Amino Acid Sequence Antigens, Surface Cell Adhesion Molecules Cloning, Molecular DNA Genetics Lectins Ultrastructure Molecular Sequence Data Receptors, Lymphocyte Homing Structure-Activity Relationship Comparative Study Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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