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

Journal Article · Sat Mar 01 00:00:00 EST 1986 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.83.5.1463· OSTI ID:5561641

Weissman, A M; Harford, J B; Svetlik, P B; Leonard, W L; Depper, J M; Waldmann, T A; Greene, W C; Klausner, R D

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.

• Research Organization: National Institutes of Health (NIH), Bethesda, MD (United States)
• OSTI ID: 5561641
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 83:5
• Country of Publication: United States
• Language: English

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