Mouse interleukin 13 (mIL-13) is a pleiotropic cytokine produced by activated Th2 cells. IL-13 induces B cell proliferation and immunoglobin production. It contains a four helical bundle with two internal disulfide bonds. Mouse IL13 shares 58% sequence identity with human protein and exhibits cross-species activity. IL13 signals via receptor IL13R (type2, IL4R) and activates STAT-6. IL13 initially binds IL-13Rα1 with low affinity and triggers association of IL4Rα, generating a high affinity heterodimeric receptor IL13R and eliciting downstream signals. IL13 also binds IL-13Rα2 with high affinity, which plays a role in a negative feedback system of IL13 signaling. IL13 is an important mediator of allergic inflammation and disease.
Mouse interleukin-16(IL-16) is a single chain non-glycosylated polypeptide. IL-16 is widely expressed in human tissues including spleen, thymus, lymph nodes, peripheral leukocytes, bone marrow and cerebellum. IL-16 plays an important role instimulating a migratory response in CD4+ lymphocytes, monocytes, and eosinophils,inducing T-lymphocyte expression of interleukin 2 receptor.It was originally identified as a CD8+ T cell-derived chemoattractant for CD4+ cells. In addition to its chemotactic properties, IL-16 has also been shown to suppress HIV-1 replication in vitro and appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. It may act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.
Interleukin-17F (IL-17F) exists in a disulfide-linked heterodimer that belongs to the IL-17 family. IL-17F is expressed in activated, but not resting, CD4+ T-cells and activated monocytes. Mouse and human IL-17F share 55% sequence identity.IL-17F has been shown to stimulate the production of several other cytokines, including IL-6, IL-8, and granulocyte colony-stimulating factor. IL-17F can regulate cartilage matrix turnover and stimulates PBMC and T-cell proliferation. IL-17F is also found to inhibit the angiogenesis of endothelial cells and induce endothelial cells to produce IL2, TGFB1/TGFB, and monocyte chemoattractant protein-1. Defects in IL-17F are the cause of familial candidiasis type 6 (CANDF6).
IL17, also known as IL17a, is a cytokine belongs to the IL-17 family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. The IL-17 family of cytokines includes six members, IL-17/IL-17A, IL-17B, IL-17C, IL-17D, IL-17E/IL-25, and IL-17F, which are produced by multiple cell types. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. This cytokine can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
Interleukin-18 (IL-18）is a protein which belongs to the IL-1 family. It is expressed as a 24 kDa precursor by endothelial and epithelial cells, keratinocytes, gamma δ T cells, and phagocytes. Mature mouse IL-18 shares 63% and 91% amino acid sequence identity with mouse and rat IL-18, respectively. IL-18 binds to the widely expressed IL-18 R alpha which recruits IL-18 R beta to form the signaling receptor complex. Its bioactivity is negatively regulated by interactions with IL-18 binding proteins and virally encoded IL-18BP homologs. It augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. In the presence of IL-12 or IL-15, IL-18 enhances anti-viral Th1 immune responses by inducing IFN-gamma production and the cytolytic activity of CD8+ T cells and NK cells. In the absence of IL-12 or IL-15, however, IL-18 promotes production of the Th2 cytokines IL-4 and IL-13 by CD4+ T cells and basophils.
Interleukin-21 also known as IL-21 is a protein that in mouse is encoded by the IL21 gene, belongs to the IL-15/IL-21 family. Interleukin-21 is a cytokine that has potent regulatory effects on cells of the immune system, including natural killer (NK) cells and cytotoxic T cells that can destroy virally infected or cancerous cells. This cytokine induces cell division/proliferation in its target cells.
Interleukin-21(IL-21) is an approximately 14 kDa cytokine which belongs to the IL-15/IL-21 family. Mature mouse IL-21 shares 66%,59%, 58%, and 88% aa sequence identity with mature canine, human, rabbit, and rat IL-21, respectively. IL-21 is produced by activated T follicular helper cells (Tfh), Th17 cells, and NKT cells. It exerts its biological effects through a heterodimeric receptor complex (IL-21 specific IL-21 R). IL-21 is a cytokine that has potent regulatory effects on cells of the immune system, including natural killer (NK) cells and cytotoxic T cells that can destroy virally infected or cancerous cells. This cytokine induces cell division/proliferation in its target cells. It is required for the migration of dendritic cells to draining lymph nodes .It co-stimulates the activation, proliferation, and survival of CD8+ T cells and NKT cells and promotes Th17 cell polarization. It blocks the generation of regulatory T cells and their suppressive effects on CD4+ T cells.
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