Fibroblast Growth Factor 21 (FGF21) is a growth factor that belongs to the FGF family. FGF family proteins play a central role during prenatal development and postnatal growth and regeneration of mamy tissues, by promoting cellular proliferation and differentiation. FGF21 is a potent activator of glucose uptake on adipocytes, protects animal from diet-induced obesity when overexpression in transgenic mice, and lower blood glucose and triglyceride levels when therapeutically adiministered to diabetic redents. FGF21 is produced by hepatocytes in reponse to free fatty acid stimulation of a PPARa/RXR dimeric complex. This situation occurs clinically during starvation, or following the ingestionof a highly-fat/low-carbohydrate diet. Upon FGF21 secretion, white adipose tissue is induced to release free fatty acids from triglyceride stores. Once free fatty acid reach hepatocytes, they are oxidized and reduced to acetyl-CoA. The acetyl-CoA is recombined into 4-carbon ketone bodies, release, and transported to peripheral tissue for TCA processing and energy generation.
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.
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