FLT3L, also known as flt3 ligand, is a small molecule that acts as a growth factor that increases the number of immune cells by activating the hematopoietic progenitors. In vivo, FLT3L also induces the mobilization of the hematopoietic progenitors and stem cells. This may help the system to kill cancer cells. Dendritic cells (DCs) provide the key link between innate and adaptive immunity by recognizing pathogens and priming pathogen-specific immune responses. FLT3L controls the development of DCs and is particularly important for plasmacytoid DCs and CD8-positive classical DCs and their CD103-positive tissue counterparts.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD135, also known as FLT-3, FLK-2, is a member of the CD system. CD135 is an important cell surface marker recognized by specific sets of antibodies to identify the types of hematopoietic (blood) progenitors in the bone marrow and it function to differentiate hematopoietic stem cells, which are CD135 negative, from multipotent progenitors, which are CD135 positive. CD135 is a receptor tyrosine kinase typeⅢ for the cytokine Flt3 ligand and activat signaling through second messengers by binding to Flt3. Signaling through CD135 is important for lymphocyte development. The encoding gene CD135 is a proto-oncogene to which mutations happened will lead to cancer such as leukemia.
Fn14 (tumor necrosis factor receptor superfamily, member 12A), also known as TNFRSF12A, is the receptor for TNFSF12/TWEAK. Fn14 shares 82% amino acid identity with the mouse sequence. It contains a signal peptide, an extracellular domain, a membrane-anchoring domain, and a cytoplasmic domain. In response to FGF1, calf serum, or phorbol ester stimulation of human quiescent fibroblasts in vitro, the level of Fn14 is increased. A 1.2-kb FN14 transcript was expressed at high levels in heart, placenta, and kidney, at intermediate levels in lung, skeletal muscle, and pancreas, and at low levels in brain and liver. In addition, elevated FN14 expression was found in human liver cancer cell lines and hepatocellular carcinoma specimens. Expression of mouse Fn14 was upregulated in hepatocellular carcinoma nodules that develop in 2 different transgenic mouse models of hepatocarcinogenesis. TNFRSF12A is the weak inducer of apoptosis in some cell types. It promotes angiogenesis and the proliferation of endothelial cells. TNFRSF12A may modulate cellular adhesion to matrix proteins.
Tumor necrosis factor receptor superfamily member 12A(TNFRSF12A) is also known as Fibroblast growth factor-inducible immediate-early response protein 14, FN14, CD266 antigen and tweak-receptor. TNFRSF12A is a single-pass type I membrane protein, including a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. TNFRSF12A is highly expressed in heart, placenta and kidney. TNFRSF12A can be induced by FGF1 and phorbol ester. TNFRSF12A binds to TWEAK/TNFSF12A to initiate a signal transduction cascade, causing different cellular responses such as cell death, cell proliferation, and angiogenesis.
Fibronectin (FN) is a glycoprotein component of the extracellular matrix of the extracellular matrix (ECM) with roles in embryogenesis, development, and wound healing. More recently, FN has emerged as player in platelet thrombus formation and diseases associated with thrombosis including vascular remodeling, atherosclerosis, and cardiac repair following a myocardial infarct. Each monomer of FN consists of three types of homologous repeating units, that is 12 type I repeats, two type II repeats and 15-17 type III repeats. The occurrence of multiple isoforms results from alternative mRNA splicing of the ED-A, ED-B and III-CS regions, and subsequent post-translational modification. As an ECM component and one of the primary cell adhesion molecules, Fibronectin can be a ligand for fibrin, heparin, chondroitin sulfate, collagen/gelatin, as well as many integrin receptors throμgh which FN mediates the variety of cellular signaling pathways. The study of solid human tumors showed among the early signs of malignant transformation the fragmentation of pericellular FN, concommitent with the increase of its production by the peritumoral stroma. These results should encourage further investigations concerning the potential importance of Fn production and brea KDown during cancer progression. FN1 expression has been described to increase significantly from the morula towards the early blastocyst stage, sμggesting that FN1 may also be involved in early blastocyst formation. The fragment 2 of FN comprises the first 7 FN type III repeats and is sμggested to be important for self association during fibril growth via the key module III2.
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