Only high-affinity receptors for interleukin 2 mediate internalization of ligand
| Autor: | Warner C. Greene, Penny B. Svetlik, Richard D. Klausner, Warren L. Leonard, Thomas A. Waldmann, Allan M. Weissman, Joel M. Depper, Joe B. Harford |
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| Rok vydání: | 1986 |
| Předmět: |
Interleukin 2
Multidisciplinary Ligand media_common.quotation_subject Lymphokine Antibodies Monoclonal Receptors Interleukin-2 Antigen-Antibody Complex Biology Endocytosis Molecular biology Membrane protein medicine Humans Interleukin-2 Cytotoxic T cell Receptors Immunologic Receptor Internalization Research Article medicine.drug media_common |
| Zdroj: | Proceedings of the National Academy of Sciences. 83:1463-1466 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.83.5.1463 |
| Popis: | Interleukin 2 (IL-2) receptors are expressed on activated T cells and in select T-cell leukemias. Recently, it has been demonstrated that at least two classes of receptor for IL-2 exist with markedly different affinities for ligand. All known biological actions of IL-2 have been correlated with occupancy of high-affinity sites; the function of the low-affinity sites remains unknown. Receptor-mediated endocytosis is the primary means of internalization of cell-surface receptors and their ligands. The internalization of IL-2 bound to high- and low-affinity receptor sites was studied in a human T-cell lymphotrophic virus type 1 (HTLV-1)-infected human T-cell leukemia cell line and in a cloned murine cytotoxic T-cell line (CTLL). Internalization of IL-2 occurred only when bound to high-affinity sites. In addition, an anti-receptor antibody (anti-Tac), which binds equally well to high- and low-affinity sites, demonstrated no detectable internalization. The implications of these findings as they relate to IL-2 receptor structure and function are discussed. |
| Databáze: | OpenAIRE |
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