ArticleProceedings of the National Academy of Sciences of the United States of America1987
The p75 peptide is the receptor for interleukin 2 expressed on large granular lymphocytes and is responsible for the interleukin 2 activation of these cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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57 citing papers in PubMed, 222 citations in OpenAlex.
- Cord Blood Mononuclear Cells Have a Potential to Produce NK Cells Using IL2Rg Cytokines.Advanced pharmaceutical bulletin · 2016Article
- Combination strategies to enhance antitumor ADCC.Immunotherapy · 2012Review
- Role of common-gamma chain cytokines in NK cell development and function: perspectives for immunotherapy.Journal of biomedicine & biotechnology · 2011Review
- Preclinical and phase I clinical trial of blockade of IL-15 using Mikbeta1 monoclonal antibody in T cell large granular lymphocyte leukemia.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- The contrasting roles of IL-2 and IL-15 in the life and death of lymphocytes: implications for the immunotherapy of rheumatological diseases.Arthritis research · 2002Review
- Expression and functional activity of the very late activation antigen-4 molecule on human natural killer cells in different states of activation.Immunology · 2000Article
- Induction by interleukin-15 of human killer cell activity against lung cancer cell lines and its regulatory mechanisms.Japanese journal of cancer research : Gann · 1996Article
- Quantitation of IL-2Rp75 (CD122) expression on mononuclear cells in rheumatic disease.Annals of the rheumatic diseases · 1996Article
- Article
- Membrane-bound/soluble IL-2 receptor (IL-2R) and levels of IL-1 alpha, IL-2, and IL-6 in the serum and in the PBMC culture supernatants from 17 patients with hematological malignancies.Cell biophysics · 1995Article
- IL-2 and IL-7 but not IL-12 protect natural killer cells from death by apoptosis and up-regulate bcl-2 expression.Immunology · 1995Article
- BY55 monoclonal antibody delineates within human cord blood and bone marrow lymphocytes distinct cell subsets mediating cytotoxic activity.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Study of IL-2 receptor expression after chemoimmunotherapy in patients treated for metastatic malignant melanoma.Clinical and experimental immunology · 1994Article
- Expression of p75 chain of IL-2 receptor in the early immunological reconstitution after allogeneic bone marrow transplantation.Clinical and experimental immunology · 1994Article
- Antigen recognition and activation of ovine gamma delta T cells.Immunology · 1994Article
- The interleukin (IL) 2 receptor beta chain is shared by IL-2 and a cytokine, provisionally designated IL-T, that stimulates T-cell proliferation and the induction of lymphokine-activated killer cells.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Characterization of the human interleukin-2 receptor beta-chain gene promoter: regulation of promoter activity by ets gene products.Molecular and cellular biology · 1993Article
- Association of p56lck with IL-2 receptor beta chain is critical for the IL-2-induced activation of p56lck.The EMBO journal · 1993Article
- Article
- The interleukin 2 receptor (IL-2R): the IL-2R alpha subunit alters the function of the IL-2R beta subunit to enhance IL-2 binding and signaling by mechanisms that do not require binding of IL-2 to IL-2R alpha subunit.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
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8 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
There are at least two interleukin 2 (IL-2) binding peptides: one is the Mr 55,000 peptide (p55) reactive with the anti-Tac monoclonal antibody, and the other is a Mr 75,000 non-Tac IL-2 binding peptide (p75). Independently existing Tac or p75 peptides represent low-affinity IL-2 receptors, whereas high-affinity IL-2 receptors are expressed when both peptides are present and associated in a receptor complex. It has long been known that normal large granular lymphocytes (LGL) or leukemic cells from the patients with abnormal expansions of LGL can be activated by IL-2 not only to more-potent natural killer cells but also to effectors of lymphokine-activated killer (LAK) activity, although they do not express the Tac peptide. In the present study, using cross-linking methodology, we found that normal LGL and leukemic LGL from all individuals tested expressed the p75 IL-2 binding peptide but did not express the Tac peptide. These LGL leukemia cells made proliferative responses to IL-2 but required a much higher concentration than that required for the proliferation of normal phytohemagglutinin-stimulated T lymphoblasts that express high-affinity receptors. Furthermore, the addition of IL-2 to Tac-negative LGL leukemic cells augmented transcription of the Tac gene and induced the Tac peptide. Neither the IL-2-induced proliferation nor the up-regulation of Tac gene expression was inhibited by the addition of anti-Tac. These results strongly suggest that the p75 peptide is responsible for IL-2-induced activation of LGL and that the p75 peptide alone can mediate an IL-2 signal. Thus, the p75 peptide may play an important role in the IL-2-mediated immune response not only by participating with the Tac peptide in the formation of the high-affinity receptor complex on T cells but also by contributing to the initial triggering of LGL activation so that these cells become efficient natural killer and lymphokine-activated killer cells.
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