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A 100-kilodalton protein is associated with the murine interleukin 2 receptor: Biochemical evidence that p100 is distinct from the. alpha. and. beta. chains

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
; ;  [1]
  1. National Institutes of Health, Bethesda, MD (USA)
Two proteins that specifically bind the T-cell growth factor interleukin 2 (IL-2) have been identified previously on the surface of T cells; these proteins have been designated IL-2R{alpha} and IL-2R{beta} for the {alpha} and {beta} chains of the IL-2 receptor (IL-2R). The association of these independent binding proteins with each other on the surface of activated T cells correlates with the generation of high-affinity binding sites. These high-affinity sites transduce the major mitogenic signal of IL-2, yet the mechanisms of association of the {alpha} and {beta} chains with each other as well as signal transduction in response to IL-2 are unknown. Cotransfection experiments of cDNAs encoding the {alpha} and {beta} chains in T cells and fibroblasts have suggested functional requirements for other T cell-specific factor(s). The authors now provide biochemical evidence for a distinct 100-kDa protein that interacts with the {alpha} or {beta} chains, or both, on the surface of the IL-2-dependent cell line CTLL-2 as well as activated murine splenocytes. This same 100-kDa protein is capable of being chemically cross-linked to {sup 125}I-labeled IL-2.
OSTI ID:
6151602
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 87:12; ISSN PNASA; ISSN 0027-8424
Country of Publication:
United States
Language:
English