Interleukin-4 (IL-4) is a pleiotropic cytokine that regulates diverse T and B cell responses including cell proliferation, survival and gene expression. IL-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of naive CD4+ T cells into helper Th2 cells, characterized by their cytokine-secretion profile that includes secretion of IL-4, IL-5, IL-6, IL-10, and IL-13, which favor a humoral immune response. Another dominant function of IL-4 is the regulation of immunoglobulin class switching to the IgG1 and IgE isotypes. Excessive IL-4 production by Th2 cells has been associated with elevated IgE production and allergic response.
IL-5 is expressed in eosinophils, NK cells, TC2 CD8+ T cells, mast cells, CD45+ CD4+ T cells, gamma delta T cells and IL-1 beta activated endothelial cells. IL-5 acts as a growth and differentiation factor for both B cells and eosinophils. Relative to B cells, IL-5 appears to induce the differentiation of activated conventional B-2 cells into Ig-secreting cells. In addition, it induces the growth of B-1 progenitors as well as IgM production by B-1 cells.IL-5 appears to perform a number of functions on eosinophils. These include the down modulation of Mac-1,the upregulation of receptors for IgA and IgG,the stimulation of lipid mediator (leukotriene C4 and PAF) secretion and the induction of granule release.IL-5 also promotes the growth and differentiation of eosinophils.
Interleukin-6 (IL-6) is a pro-inflammatory cytokine that also has an important role in immunity. Mouse IL-6 appears to be directly involved in the responses that occur after infection and injury and may prove to be as important as IL-1 in regulating the acute phase response. Mouse IL-6 is reported to be produced by fibroblasts, activated T cells, activated monocytes or macrophages, and endothelial cells. It acts upon a variety of cells, including fibroblasts, myeloid progenitor cells, T cells, B cells and hepatocytes. IL-6 has a wide variety of biological functions: it plays an essential role in the final differentiation of B-cells into Ig-secreting cells, it induces myeloma and plasmacytoma growth, nerve cells differentiation in hepatocytes, and acute phase reactants.
IL7, also known as interleukin 7, is a hematopoietic growth factor that belongs to the IL-7/IL-9 family. It is secreted by stromal cells in the bone marrow and thymus. IL7 stimulates the proliferation of lymphoid progenitors. It is important for proliferation during certain stages of B-cell maturation. IL7 and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. It is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRß) during early T cell development. IL7 can be produced locally by intestinal epithelial and epithelial goblet cells and may serve as a regulatory factor for intestinal mucosal lymphocytes.
Interleukin-9 (IL-9) is a secreted protein that belongs to the IL-7/IL-9 family.Mature mouse IL-9 shares 57% and 74% amino acid sequence identity with human and rat IL-9, respectively. IL-9 supports IL-2 independent and IL-4 independent growth of helper T-cells. IL-9 stimulates cell proliferation and prevents apoptosis. It functions through the IL-9 receptor (IL-9R), which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. IL-9 has been identified as a candidate gene for asthma. IL-9 is a determining factor in the pathogenesis of bronchial hyperresponsiveness.
IL-2-inducible T cell kinase is a member of the protein kinase superfamily, Tyr protein kinase family and TEC subfamily. It contains 1 Btk-type zinc finger, 1 PH domain, 1 protein kinase domain, 1 SH2 domain and 1 SH3 domain. As an intracellular kinase which expressed in T-cells, IL-2-inducible T cell kinase contains both SH2 and SH3 domains which are often found in intracellular kinases. It is hought to play a role in T-cell proliferation and differentiation. It regulates the development, function and differentiation of conventional T-cells and nonconventional NKT-cells. IL-2-inducible T cell kinase also plays an essential role in regulation of the adaptive immune response. efects in IL-2-inducible T cell kinase are the cause of lymphoproliferative syndrome EBV-associated autosomal type 1 (LPSA1). LPSA1 is a rare immunodeficiency characterized by extreme susceptibility to infection with Epstein-Barr virus (EBV). Inadequate immune response to EBV can have a fatal outcome. Clinical features include splenomegaly, lymphadenopathy, anemia, thrombocytopenia, pancytopenia, recurrent infections. There is an increased risk for lymphoma.
Junctional adhesion molecule B (JAM-B), also known as Junctional adhesion molecule 2 (JAM2), Vascular endothelial junction-associated molecule (VE-JAM), and CD322, is a single-pass type I membrane protein which belongs to the immunoglobulin superfamily. It is prominently expressed on high endothelial venules. expression to be restricted to the high endothelial venule of tonsil and lymph nodes. The localization to the endothelium of arterioles in and around inflammatory and tumor foci. JAM-B can function as an adhesive ligand for the T cell line J45 and can interact with GM-CSF/IL-4-derived peripheral blood dendritic cells, circulating CD56(+) NK cells, circulating CD56(+)CD3(+) NK/T cells, and circulating CD56(+)CD3(+)CD8(+) cytolytic T cells. JAM-2 is expressed on high endothelial venules (HEVs) in human tonsil and on a subset of human leukocytes, suggesting that JAM-2 plays a central role in the regulation of transendothelial migration. It binds to very late activation antigen (VLA)-4, a leucocyte integrin that contributes to rolling and firm adhesion of lymphocytes to endothelial cells through binding to vascular cell adhesion molecule (VCAM)-1. JAM-B appears to contribute to leucocyte extravasation by facilitating not only transmigration but also rolling and adhesion. JAM-B acts as an adhesive ligand for interacting with a variety of immune cell types and may play a role in lymphocyte homing to secondary lymphoid organs.
Junctional Adhesion Molecule C Protein & Antibody (JAM-C, JAM3 Protein) also known as Junctional adhesion molecule 3, JAM3, is a single-pass type I membrane protein that belongs to the immunoglobulin superfamily. It is an adhesion molecule expressed by endothelial cells (ECs) that plays a role in tight junction formation, leukocyte adhesion, and transendothelial migration. JAM-C is an adhesion molecule that is expressed on cells within the vascular compartment and epithelial cells and, to date, has been largely studied in the context of inflammatory events. JAM-C is also expressed in peripheral nerves and that this expression is localized to Schwann cells at junctions between adjoining myelin end loops. JAM-C was recently shown to be a counter receptor for the leukocyte beta2-integrin Mac-1 (CD11b/CD18), thereby mediating interactions between vascular cells, particularly in inflammatory cell recruitment. JAM-C is up-regulated by oxidized low-density lipoprotein (LDL) and may thereby contribute to increased inflammatory cell recruitment during atherosclerosis. JAM-C may therefore provide a novel molecular target for antagonizing interactions between vascular cells in atherosclerosis. JAM-C was shown to undergo a heterophilic interaction with the leukocyte beta2 integrin Mac-1, thereby mediating interactions between vascular cells in inflammatory cell recruitment. The homophilic interaction of JAM-C can mediate tumor cell-endothelial cell interactions and may thereby be involved in the process of tumor cell metastasis.
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