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

نویسندگان

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

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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عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 83 5  شماره 

صفحات  -

تاریخ انتشار 1986