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. 1986 Mar;83(5):1463–1466. doi: 10.1073/pnas.83.5.1463

Only high-affinity receptors for interleukin 2 mediate internalization of ligand.

A M Weissman, J B Harford, P B Svetlik, W L Leonard, J M Depper, T A Waldmann, W C Greene, R D Klausner
PMCID: PMC323096  PMID: 3081898

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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