psoriasis-associated

Fatty acid-binding protein 5 (FABP5) is a cytoplasm protein that belongs to the fatty-acid binding protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP5 can be expressed in keratinocytes, and is highly expressed in psoriatic skin. FABP5 has been shown to be involved in keratinocyte differentiation. FABP5 has high specificity for fatty acids, the highest affinity for C18 chain length. FABP5 can decrease the chain length or introduce double bonds to reduce the affinity.

Fatty acid-binding protein, also known as Epidermal-type fatty acid-binding protein, Fatty acid-binding protein 5, Psoriasis-associated fatty acid-binding protein homolog, E-FABP and FABP5, is a cytoplasm protein which Belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid-binding proteins ( FABPs ) are postulated to serve as lipid shuttles that solubilize hydrophobic fatty acids and deliver them to appropriate intracellular sites. E-FABP / FABP5 is predominantly expressed in keratinocytes and is overexpressed in the actively proliferating tissue characteristic of psoriasis and wound healing. E-FABP / FABP5 exhibits an important role in binding free fatty acids, as well as regulating lipid metabolism and transport. E-FABP / FABP5 has high specificity for fatty acids. It has highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity of FABP5. E-FABP / FABP5 may be involved in keratinocyte differentiation.

IL-21 and IL-21R were highly expressed in the lesional skin and peripheral blood of psoriasis patients. IL-21 promoted CD4 T cells proliferation and Th17 cells differentiation and inhibiting Treg cells differentiation by upregulating RORγt expression and downregulating Foxp3 expression, with increased expression and secretion of IL-17A and IL-22.Microbial translocation and the associated immune activation during HIV-1 infection may lead to high expression levels of the IL-21R activation marker in RM B cells, a feature associated with increased apoptosis and a reduced number of these cells in the circulation.

Lymphotoxin-alpha, also known as LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA TNFSF1, and TNFB, is a secreted protein that belongs to the tumor necrosis factor family. TNF-beta/TNFSF1/Lymphotoxin alpha is highly inducible, secreted, and exists as a homotrimeric molecule. It is a cytokine that in its homotrimeric form binds to TNFRSF1A / TNFR1, TNFRSF1B / TNFBR, and TNFRSF14 / HVEM. In its heterotrimeric form with LTB, TNF-beta/TNFSF1/Lymphotoxin alpha binds to TNFRSF3 / LTBR. Lymphotoxin is produced by lymphocytes and cytotoxic for a wide range of tumor cells. TNF-beta/TNFSF1/Lymphotoxin alpha forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. It mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. TNF-beta/TNFSF1/Lymphotoxin alpha is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis. Genetic variations in TNF-beta/TNFSF1/Lymphotoxin alpha are a cause of susceptibility psoriatic arthritis which is an inflammatory, seronegative arthritis associated with psoriasis. It is a heterogeneous disorder ranging from a mild, non-destructive disease to a severe, progressive, erosive arthropathy.

Interleukin 23 receptor (IL23R) is a type I cytokine receptor for IL23. IL23 receptor complex is comprised of two subunits, the IL12Rβ1 subunit, which is shared with several cytokines, and a subunit that is unique to IL-23. IL23, after binding to IL23R, activates memory T cells and mediates pro-inflammatory activities in part by the production of IL17 through activation of TH17 lymphocytes. IL23R is expressed on T cells, NK cells, dendritic cells, and macrophages. In fact, polymorphisms of the IL23R gene were reported to be associated with susceptibility to inflammatory diseases and autoimmune diseases such as psoriasis, multiple sclerosis, Graves's ophtalmopathy and inflammatory bowel diseases. The IL23R is known to be critically involved in the carcinogenesis of different malignant tumor.

Interleukin 23 receptor (IL23R), a heterodimer of the IL12 receptor β1 (IL12Rβ1) and IL12Rβ2, is a type I cytokine receptor for IL23. IL23R is comprised of two subunits, the IL12Rβ1 subunit, which is shared with several cytokines, and a subunit that is unique to IL-23. IL23, after binding to IL23R, activates memory T cells and mediates pro-inflammatory activities in part by the production of IL17 through activation of TH17 lymphocytes. IL23R is expressed on T cells, NK cells, dendritic cells, and macrophages. In fact, polymorphisms of the IL23R gene were reported to be associated with susceptibility to inflammatory diseases and autoimmune diseases such as psoriasis, multiple sclerosis, Graves's ophtalmopathy and inflammatory bowel diseases. The IL23R is known to be critically involved in the carcinogenesis of different malignant tumor.