Hepassocin, also known as hepatocyte-derived fibrinogen-related protein 1 (HFREP-1), is a liver-specific secreted protein belonging to the fibronogen superfamily, whose members share a fibrinogen domain at their C-termini. It is secreted by the liver and functions as a mitogen for hepatocytes. Hepassocin may play a role in the development of hepatocellular carcinomas. Hepassocin is a disulfide-linked homodimeric protein with a C-terminal fibrinogen domain. It is reported that it is a major immune inhibitory ligand of LAG-3 .
Fibrinogen-like protein 1(FGL1) is also known as HP-041, Hepassocin, HFREP-1, LFIRE-1, is a liver-specific secreted protein belonging to the fibronogen superfamily, whose members share a fibrinogen domain at their C-termini. It is secreted by the liver and functions as a mitogen for hepatocytes. Hepassocin may play a role in the development of hepatocellular carcinomas. Hepassocin is a disulfide-linked homodimeric protein with a C-terminal fibrinogen domain. It is reported that it is a major immune inhibitory ligand of LAG-3.
TNFSF18 is a single-pass type II membrane protein. It is expressed at high levels in the small intestine, ovary, testis, kidney and endothelial cells. TNFSF18 cytokine binds to TNFRSF18/AITR/GITR. It regulates T-cell responses, and functions as costimulator and lower the threshold for T-cell activation and T-cell proliferation. It is Important for interactions between activated T-lymphocytes and endothelial cells and Promotes leukocyte adhesion to endothelial cells. TNFSF18 mediates activation of NF-kappa-B. As Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1. It also regulates migration of monocytes from the splenic reservoir to sites of inflammation.
CD123, also known as Interleukin-3 receptor subunit alpha, belongs to the type I cytokine receptor family. In mouse, there are two classes of high-affinity IL3 receptors. One contains an IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors. CD123 stimulates the proliferation and differentiation of hemopoietic cells including the pluripotent hematopoietic stem cells as well as various lineage-committed cells. CD123 is a heterodimer consisting of an alpha and a beta subunit. The alpha subunit alone binds IL-3 with low affinity. The beta subunit does not bind IL-3 by itself but is required for the high-affinity binding of IL-3 to the heterodimeric receptor complex.
Interleukin-4 receptor subunit alpha(IL-4RA), alos known as Soluble IL-4 receptor subunit alpha, belongs to the type I cytokine receptor family and type 4 subfamily. It expressed in both Th1 and Th2 cells. It functions as receptor for both interleukin 4 and interleukin 13 and couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and chemokine and mucus production at sites of allergic inflammation. In certain cell types, IL-4RA can signal through activation of insulin receptor substrates, IRS1/IRS2. The functional IL4 receptor is formed by initial binding of IL4 to IL4R. Subsequently it recruits to the complex of the common gamma chain. In immune cells, IL-4RA creates a type I receptor. In non-immune cells, it forms a type II receptor with of IL13RA1. IL4R can also interact with the IL13/IL13RA1 complex to form a similar type II receptor and interacts with the SH2-containing phosphatases, PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP.
Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.
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