Interleukins

Murine D17Wsu104e (SF20) is a bone marrow stroma-derived growth factor, sometimes called IL25 (not to be confused with IL17E/IL25). SF20 is expressed in bone marrow, spleen stroma cells, resting mononuclear cells, resting CD8+ and CD19+ cells and activated CD8+ T-cells. SF20 has also been shown to bind to the surface of cells expressing the receptor TSA-1 (Thymic shared Ag-1). Among its biological activities, SF20 stimulates the proliferation of FDCP2 cells (a mouse factor-dependent hemopoietic cell line) and mouse lymphoid cells.

Interferon lambda 1, also known as interleukin 29, belongs to the newly classified type III interferon family. Expression of IFNL1 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL1 exerts antiviral activity and upregulation of MHC class I antigen expression. It signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3.

Interferon lambda 2, also known as interleukin 28A, belongs to the newly classified type III interferon family. Expression of IFNL2 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL2 exerts antiviral activity by activating mx proteins, 2',5'-oligoadenylate synthetase, and interferon regulatory factor 9. It signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3.

Interleukin-10 (IL10), also known as cytokine synthesis inhibitory factor (CSIF), is the charter member of the IL10 family of F-helical cytokines that also includes IL19, IL20, IL22, IL24, and IL26/AK155. While the gene which encodes IL10 is comprised of 178 amino acids, the active protein only contains 160 amino acids. IL10 contains two intrachain disulfide bridges and is expressed as a 36 kDa noncovalently associated homodimer. The IL10 dimer binds to two IL10 RF/IL10R1 chains, resulting in the recruitment of two IL10 RH/IL10R2 chains and the activation of a signaling cascade involving JAK1, TYK2, and STAT3. IL10RH does not bind IL10 directly, but is required for signal transduction. IL10 is also a critical molecule in the control of viral infections, allergic reactions and autoimmune inflammation. IL10 promotes phagocytic uptake and Th2 responses, but suppresses antigen presentation and Th1 pro-inflammatory responses. IL10 is secreted by many activated hematopoietic cell types, as well as hepatic stellate cells, keratinocytes and placental cytotrophoblasts. Human IL10 is active on mouse cells; however mouse IL10 does not act on human cells.

Interleukin-10 (IL10) is an immunosuppressive cytokine produced by a variety of mammalian cell types including macrophages, monocytes, T-cells, B-cells and keratinocytes. IL10 inhibits the expression of pro-inflammatory cytokines such as IL1 and TNFα. Like IL4, IL10 enhances humoral immune responses and attenuates cell-mediated immune reactions. Human IL10 is active on murine cells, but murine IL10 is inactive on human cells.

Interleukin-11 (IL11) is encoded by the IL11 gene and is a member of IL6 superfamily, which is distinguished based on its use of the common co-receptor gp130. IL11 is a multifunctional cytokine that was first isolated from bone marrow-derived stromal cells. IL11 receptor activation requires the formation of a complex that contains two IL11 molecules, two molecules of the ligand-binding IL11 RF subunit, and two molecules of the expressed cell signaling G-subunit, gp130. The functions of IL11 are that it directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells, and induces megakaryocyte maturation that results in increased platelet production.

Interleukin-11 (IL11) is a pleiotropic cytokine that was originally detected in the conditioned medium of an IL1α-stimulated primate bone marrow stromal cell line (PU-34) as a mitogen for the IL6-responsive murine plasmacytoma cell line T11. IL11 contains no cysteine residues or potential glycosylation sites. IL11 has multiple effects on both hematopoietic and nonhematopoietic cells. Many of the biological effects described for IL11 overlap with those of IL6. In vitro, IL11 can synergize with IL3, IL4 and SCF to shorten the G0 period of early hematopoietic progenitors. IL11 also enhances the IL3-dependent megakaryocyte colony formation. IL11 has been found to stimulate the T-cell dependent development of specific immunoglobulin-secreting B-cells.

Human interleukin-13 (IL13) is expressed by the IL13 gene located on chromosome 5 and is secreted by many cell types, especially T-helper type 2 (Th2) cells. The high solution form of IL13 is reported to be a monomer with two internal disulfide bonds that contribute to a bundled four F-helix configuration. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development and indicated an important role for IL13 in the expulsion of gastrointestinal parasites. IL13 exerts anti-inflammatory effects on monocytes and macrophages, and can also inhibit the expression of inflammatory cytokines such as IL1beta, TNF-alpha, IL6 and IL8. IL13 has also been shown to enhance B-cell proliferation, as well as induce isotype switching, which results in an increased production of IgE. Human, mouse and rat IL13 share a low percentage of homology, but have cross species activity.

Interleukin-13 (IL13) is an immunoregulatory cytokine produced primarily by activated Th2 cells, along with mast cells and NK cells. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development and indicated that IL13 plays an important role in the expulsion of gastrointestinal parasites. IL13 exerts anti-inflammatory effects on monocytes and macrophages and inhibits the expression of inflammatory cytokines such as IL1β, TNF-α, IL6 and IL8. IL13 has also been shown to enhance B-cell proliferation and to induce isotype switching which results in an increased production of IgE. It has been suggested that the blocking of IL13 and its downstream effectors could play a role in the mechanism of asthma. Human and murine IL13 are cross-species reactive.

Interleukin 13 (IL13) is an immunoregulatory cytokine produced primarily by activated Th2-cells, mast cells and natural killer (NK) cells. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development, and indicated an important role for IL13 in the expulsion of gastrointestinal parasites. IL13 exerts anti-inflammatory effects on monocytes and macrophages, and inhibits the expression of inflammatory cytokines such as IL1β, TNF-α, IL6 and IL8. IL13 has also been shown to enhance B-cell proliferation and induce isotype switching, which results in an increased production of IgE. Blocking IL13 activity inhibits the pathophysiology of asthma.

Interleukin-13 (IL13) is expressed by the IL13 gene and secreted by many cell types, especially type 2 helper T-cells (Th2). The high solution form of IL13 has been reported to be a monomer with two internal disulfide bonds that contribute to its bundled four F-helix configuration. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development and suggested an important role for IL13 in the expulsion of gastrointestinal parasites. IL13 exerts anti-inflammatory effects on monocytes and macrophages, and it inhibits the expression of inflammatory cytokines such as IL1β, TNF-α, IL6 and IL8. IL13 has also been shown to enhance B-cell proliferation and induce isotype switching, which results in an increased production of IgE. Mature rhesus IL13 shares 95%, 59% and 60% amino acid sequence identity with human, mouse, and rat IL13, respectively.

Human interleukin-15 (IL15) is expressed by the IL15 gene located on chromosome 4. It shares approximately 97% and 73% sequence identity with simian and murine IL15, respectively. Both human IL15 and simian IL15 are active on murine cells. IL15 is secreted by mononuclear phagocytes, especially macrophages following infection by virus. It possesses a variety of biological functions that include the stimulation and maintenance of cellular immune responses, specifically the responses which regulate natural killer (NK) cell and T-cell activation and proliferation. In addition, IL15 shares many biological properties with IL2, including T, B and NK cell-stimulatory activities. IL15 signals through a complex composed of IL2/IL15 receptor beta chain. Although IL15 lacks sequence homology with IL2, it has been shown that both the beta and gamma chains of the IL2 receptor are utilized for IL15 binding and signaling. In addition, an IL15 specific binding protein has been cloned from a mouse T-cell clone.

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Human interleukin-16 (IL16) is also called lymphocyte chemoattractant factor (LCF) and it has three isoforms, which are cleaved from preinterleukin16. IL16 is mostly secreted by lymphocytes, epithelial cells, eosinophils and CD8+ T-cells. IL16 signals through the CD4 receptor, and has many functions, which include the induction of the IL2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions, and many more. Furthermore, recombinant human IL16 (121 a.a.) contains 121 amino acid residues and shares 85% amino acid sequence identity with murine IL16.

Interleukin-16 (IL16) is also called lymphocyte chemoattractant factor (LCF) and is mostly secreted by lymphocytes, epithelial cells, eosinophils and CD8+ T-cells. It has many functions, including the induction of IL2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, and the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions. IL16 produces its signal through the CD4 receptor. Furthermore, recombinant murine interleukin-16 contains 118 amino acid residues and shares about 85% amino acid sequence identity with different isoforms of human IL16.

Interleukin-16 (IL16), also called lymphocyte chemoattractant factor (LCF), is predominately secreted by lymphocytes, epithelial cells, eosinophils, and CD8+ T-cells. It has many functions, including the induction of IL-2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, and the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions. IL16 signals through the CD4 receptor. Furthermore, recombinant rhesus macaque IL16 contains 121 amino acid residues and shares 95% and 85% amino acid sequence identity with human and murine IL16, respectively.

Human interleukin-17A (IL17A) is encoded by the IL17A gene located on chromosome 6, and belongs to the IL17 family that contains IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. All of the members of the IL17 family have a similar protein structure, which includes four highly conserved cysteine residues that are critical to their 3 dimensional shape. Both recombinant and natural IL17 have been shown to exist as disulfide linked homodimers, and mature IL17 contains one potential N-linked glycosylation site. At the amino acid level, IL17 exhibits 63% amino acid identity with mouse IL17. However, there is no reported sequence similarity to any other known cytokines. IL17 is a T-cell expressed pleiotropic cytokine that exhibits a high degree of homology to a protein encoded by the ORF13 gene of the herpesvirus, Saimiri. High levels of human IL17 were induced from primary peripheral blood CD4+ T-cells upon stimulation, which can induce stromal cells to produce proinflammatory and hematopoietic cytokines.

Rat Interleukin 17A (IL17A) belongs to the IL17 family that contains IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. All of the members of the IL17 family are proinflammatory cytokines that share four conserved cysteine residues, but diverge at the N-terminus. Both recombinant and natural IL17 have been shown to exist as disulfide linked homodimers, and mature IL17 contains one potential N-linked glycosylation site. IL17 is a T-cell expressed pleiotropic cytokine that regulates the activities of NF-kappaB and mitogen-activated protein kinases, and can stimulate the expression of IL-6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO).

Human interleukin-19 (IL19) is encoded by the IL19 gene, which is located on chromosome 1. The protein belongs to the IL10 family of interleukins, which includes: IL10, IL20, IL22, IL24, and IL26. As a monomer made of seven amphipathic helices, IL19 has a helical bundle and shares the same cell surface receptor (IL20R) with IL20 and IL24. IL19 may play an important roles in inflammatory responses because it promotes the upregulation of IL6 and TNF-α, induces apoptosis, and activates the autoantibody production in B-cells.

Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological, hematopoietic activities, and plays one of the central roles in the regulation of the immune responses. Both IL1A and IL-1B bind to the same receptor and have similar biological properties. Among various species, the amino acid sequence of mature IL1A is conserved 60% to 70% and human IL1A has been found to be biologically active with murine cell lines.

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Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar biological properties. These cytokines have a broad range of activities including stimulation of thymocyte proliferation by inducing IL2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1B is a secreted cytokine, IL1A is predominantly a cell associated cytokine.