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      Interleukin-15 as a potential regulator of the innate immune response

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          Abstract

          Interleukin-15 (IL-15) is a newly-discovered cytokine that is produced by activated monocytes early in the course of the innate immune response. IL-15 is able to bind to components of the interleukin-2 receptor (IL-2R) despite the fact that it has no sequence homology with IL-2. IL-15 stimulates human natural killer cell proliferation, cytotoxicity, and cytokine production and can substitute for IL-2 under most conditions. In vitro studies indicate that monocyte-derived IL-15 may be an important determinant of IFN-gamma production by NK cells. In addition, IL-15 is able to promote the survival of natural killer cells under serum-free conditions. The IL-15 receptor is a heterotrimeric complex which is composed of the IL-2Rß and <FONT FACE="Symbol">g</font> chains in combination with a unique alpha chain (IL-15<FONT FACE="Symbol">a</font>). The IL-15R<FONT FACE="Symbol">a</font> chain has strong sequence homology to the IL-2R<FONT FACE="Symbol">a</font> chain and confers high affinity binding to the IL-15R. In contrast to IL-2, transcript for IL-15 and IL-15<FONT FACE="Symbol">a</font> is expressed in a number of tissues and indicates that IL-15 may be an important ligand for cells that express components of the IL-2R

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          Most cited references26

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          The role of shared receptor motifs and common Stat proteins in the generation of cytokine pleiotropy and redundancy by IL-2, IL-4, IL-7, IL-13, and IL-15.

          To understand the molecular bases for cytokine redundancy and pleiotropy, we have compared the Stat proteins activated in peripheral blood lymphocytes (PBLs) by cytokines with shared and distinct actions. Interleukin-2 (IL-2) rapidly activated Stat5 in fresh PBL, and Stat3 and Stat5 in preactivated PBL. IL-7 and IL-15 induced the same complexes as IL-2, a feature explained by the existence of similar tyrosine-phosphorylated motifs in the cytoplasmic domains of IL-2R beta and IL-7R that can serve as docking sites for Stat proteins. IL-13 Induced the same complexes as IL-4, a finding explained by our studies implicating IL-4R as a shared component of the receptors. These studies demonstrate that a single cytokine can activate different combinations of Stat proteins under different physiological conditions, and also indicate two mechanisms by which distinct cytokines can activate the same Stat protein.
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            Interleukin-2: inception, impact, and implications

            K. Smith (1988)
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              Biology and clinical relevance of human natural killer cells.

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                Author and article information

                Journal
                bjmbr
                Brazilian Journal of Medical and Biological Research
                Braz J Med Biol Res
                Associação Brasileira de Divulgação Científica (Ribeirão Preto, SP, Brazil )
                0100-879X
                1414-431X
                January 1998
                : 31
                : 1
                : 1-9
                Affiliations
                [01] orgname orgdiv1 Surgery
                [02] orgnameRoswell Park Cancer Institute orgdiv1 Medicine
                Article
                S0100-879X1998000100001 S0100-879X(98)03100101
                10.1590/S0100-879X1998000100001
                d75d4058-50c1-4dbb-8bc8-78d3ac78c87a

                This work is licensed under a Creative Commons Attribution 4.0 International License.

                History
                : 24 September 1997
                : 04 September 1997
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 26, Pages: 9
                Product

                SciELO Brazil

                Categories
                Growth factor

                innate immunity,natural killer cell,gamma interferon,interleukin-12,interleukin-15

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