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Facts about Tumor necrosis factor.
Impairs regulatory T- cells (Treg) function in people with rheumatoid arthritis through FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and producing Treg cells functionally defective (PubMed:23396208).
Human | |
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Gene Name: | TNF |
Uniprot: | P01375 |
Entrez: | 7124 |
Belongs to: |
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Tumor necrosis factor family |
APC1 protein; Cachectin; Cachetin; DIF; TNF; TNF, monocyte-derived; TNFA; TNF-A; TNFalpha; TNF-alpha; TNF-alphacachectin; TNFATNF, macrophage-derived; TNFG1F; TNFSF1A; TNFSF2; TNFSF2TNF superfamily, member 2; tumor necrosis factor (TNF superfamily, member 2); tumor necrosis factor alpha; Tumor necrosis factor ligand superfamily member 2; tumor necrosis factor; tumor necrosis factor-alpha
Mass (kDA):
25.644 kDA
Human | |
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Location: | 6p21.33 |
Sequence: | Chromosome 6; NC_000006.12 (31575565..31578336) |
Cell membrane; Single-pass type II membrane protein.; [Tumor necrosis factor, membrane form]: Membrane; Single-pass type II membrane protein.; [Tumor necrosis factor, soluble form]: Secreted.; [C-domain 1]: Secreted.; [C-domain 2]: Secreted.
Boster Bio's TNF Marker is an excellent product. You've probably read about articles about cell adhesion. You might also have heard about Fibronectin and Macrophage markers. Let's now take a look at their significance for educators. Below are a few of the most effective uses of the TNF Marker.
The Boster Bio Anti-TNF Alpha Monoclonal antibody reacts with mouse, human and rabbit TNF. It is compatible with several species. This antibody can be used to recognize various proteins in ex vivo. The Boster Bio TNF Marker is validated for various applications in immunohistochemistry, molecular biology, and cytometry. Researchers can use this antibody for clinical trials, research as well as a variety of laboratory applications.
Fibronectin is one of the proteins found in the extracellular matrix (ECM). Fibronectin is released by cells that contain fibroblasts. It is thought that fibronectin is involved in cell adhesion, growth, migration, and differentiation. Complex cell-mediated processes lead to the fibronectin becoming an insoluble matrix. It is also involved in many functions in the body.
TNF-a, FN and FN interact to promote cell adhesion. TNF-a and FN interact by binding to their amino-terminal regions. This interaction encourages CD4+ T-cell adhesion. Laminin and TNF-a interactions also enhance T cell adhesion. This interaction is believed to have a limited effect on adhesion however it is believed that it facilitates T cell growth and migration.
In addition to its function in the inflammation response, fibronectin is a major factor in the development of cancer. Lung cancer expresses fibronectin. These cancer cells adhere to fibronectin, increasing their tumorigenicity, and conferring resistance to apoptosis-inducing agents. Fibronectin also enhances vertebrateandrogen (which regulates the cyclin D) expression. Fibronectin may represent a potential new target for anticancer drugs.
TNF-a and FN have been demonstrated to inhibit the expression of MMP-9 in monocytes. Fibronectin is one of the components of the ECM that plays a biological function in the introduction of cytokines and leukocytes during cell migration. Fibronectin as well as the TNF marker are also vital markers for fibronectin and TNF-a, which allows researchers to comprehend how they function together.
This study has shown that FN/TNF/a interactions are different from those involving sTNF/a FN substrates. TNF-a also was found to interact with FN-b1 integrin in order to facilitate adhesion. It is not clear whether TNF-a plays a role in activation of MMP-9.
TNF marker is a biological marker created by various types of cells. It is especially beneficial for research because it can detect a wide range of biological phenomena, including inflammation and infection. The marker can be used for a wide spectrum of applications, including research into cancer, cardiovascular disease inflammation in the gastrointestinal tract, and inflammation in the brain. However, it does have some limitations. To identify the most suitable applications for the TNF marker, researchers have to know the nature of the disease and how it manifests.
TNF-alpha is a cell signaling protein regulates inflammatory response. It is present in the serum of healthy individuals and is produced by macrophages, monocytes, and macrophages. In the body the TNF-alpha protein is processed by a metalloprotease enzyme to create a protein of 17 kDa. It is a homotrimer and can form polymers. TNF-alpha can also be detected through Western Blots that contain specific antibodies.
Despite its tiny size, plasma-fibronectin plays an important role in cell adhesion and migration. N-glycans from this protein are thought to regulate cell adhesion and movement by stimulating integrin-mediated adhesive signals. In addition, fibronectin functions as a glial-like proteins that is found in the cytoplasm of all cells.
In vitro analysis of U2OS cells' concentrations was done to determine if fibronectin is necessary for adhesion of cells. After plating the cells on a coverlip containing the indicated amount of fibronectin was applied after which the cells were stained with paxillin. These images were used to calculate the area of focal adhesions outlined by paxillin within a cell. Similar to fibronectin's effect on cell adhesion and migration in vivo was evaluated by comparing the level of fibronectin versus the control without it.
Human alveolar macrophages release fibronectin and localize it to areas of attachment in the cell membrane. It attaches to gelatin coated latex particles. Trypsin is the catalyst that activates it. Adult mesentery epithelial cells synthesize large quantities of fibronectin and arrange intracellular microfilament bundles.
In vitro experiments show that fibronectin sequences of protein from porcine and human cells have high identity (94%) which suggests similar capabilities in cell adhesion and migration and growth. Furthermore, both fibronectins are able to be isolated and show similar wound-closure effects. Fibronectin is essential for cell adhesion as well as migration. It also has important therapeutic implications. Its role in adhesion of cells has been extensively studied in the field of human cancer research.
The study of fibronectin's role in cell adhesin has demonstrated that porcine and homo fibronectins have similar abilities to regulate the strength and the organization of F-actin. Fibronectin promotes cell adhesion by activating F-actin as well as a4b1 integrin cells to stick to the fibronectin-coated surface.
Cells migrate when there is no cytoskeletal system. Instead they join to a scaffold made of fibronectin. Cells attach themselves to the scaffold by pulling on its integrin receptors. As cells pull on the scaffold, fibronectin gets unveiled, revealing a location for polymerization and assembly. This creates a network of fibrils that are branched.
Fibronectin is a protein that can be synthesized to stimulate cell growth in a variety of ways. Fibronectin can be used to stimulate the migration of SAECs in a biphasic fashion, for example. Artificial fibronectin can be used as an anti-inflammatory medicine and eye drops are used to stimulate wound healing. Fibronectin could also be synthesized into peptides that stop unwanted processes.
The interaction between PDGF-AA and PDGF is likely to occur in embryos in development of Xenopus. However this study suggests that the cell-based migration substrate is an ECM which contains fibrinonectin. However, this interaction does not seem to be a mandatory prerequisite for migration. It is believed to be a consequence of the binding of PDGFAA to the fibronectin.
Fibronectin is an extracellular matrix glycoprotein that has multiple functions that interacts with cell surface receptors. It is produced by various cells and released as a disulfide-bonded dimer. It is composed of three modular consensus amino acid sequences and one variable region. It is able to interact with glycosaminoglycans, complement, or connect to the cell's surface. The exact mechanism behind this interaction remains a mystery.
Fibronectin polymerization enhances the cytoskeletal organization of actin. Actin filament reorganization is required to extend and traction during cell migration. Thus, fibronectin plays an essential role in cell mobility. Fibronectin also plays a role in cell migration and is important in the life of the host tissue. It is important to determine the receptors for fibronectin so that we can better understand the role played by fibronectin in cell migration.
Aggarwal, B.B. (2003). Signalling pathways of the TNF superfamily: a double-edged sword. Nature Reviews Immunology, 3, 745-756. doi: 10.1038/nri1184
Aggarwal, B.B., Moffat, B., & Harkins, R.N. (1984). Human lymphotoxin. Production by a lymphoblastoid cell line, purification, and initial characterization. Journal of Biological Chemistry, 259(1), 686-691.
Balkwill, F. (2006). TNF-alpha in promotion and progression of cancer. Cancer Metastasis Reviews, 25. doi: 10.1007/s10555-006-9005-3
Carswell, E.A., Old, L.J., Kassel, R.L., Green, S., Fiore, N., & Williamson, B. (1975). An endotoxin-induced serum factor that causes necrosis of tumors. Proceedings of the National Academy of Sciences of the United States of America, 72(9), 3666-3670. doi: 10.1073/pnas.72.9.3666
Diwan, A., Tran, T., Misra, A., & Mann, D.L. (2003). Inflammatory mediators and the failing heart: a translational approach. Current Molecular Medicine, 3(2), 161-182. doi: 10.2174/1566524033361537
Dowlati, Y., Herrmann, N., Swardfager, W., Liu, H., Sham, L., Reim, E.K., & Lanctot, K.L. (2010). A meta-analysis of cytokines in major depression. Biological Psychiatry, 67(5), 446-457. doi: 10.1016/j.biopsych.2009.09.033
Hehlgans, T., & Pfeffer, K. (2005). The intriguing biology of the tumour necrosis factor/tumour necrosis factor receptor superfamily: players, rules and the games. Immunology, 115(1), 1-20. doi: 10.1111/j.1365-2567.2005.02143.x
Horiuchi, T., Mitoma, H., Harashima, S., Tsukamoto, H., & Shimoda, T. (2010). Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents. Rheumatology (Oxford), 49(7), 1215-1228. doi: 10.1093/rheumatology/keq031
Lee, S.Y., Ju, M.K., Jeon, H.M., Jeong, E.K., Lee, Y.J., Kim, C.H..,?, Kang, H.S. (2018). Regulation of Tumor Progression by Programmed Necrosis. Oxidative Medicine and Cellular Longevity, 2018. doi: 10.1155/2018/3537471
Levine, B., Kalman, J., Mayer, L., Fillit, H.M., & Packer, M. (1990). Elevated circulating levels of tumor necrosis factor in severe chronic heart failure. New England Journal of Medicine, 323(4), 236-241. doi: 10.1056/NEJM199007263230405
Nagatsu, T., & Sawada, M. (2005). Inflammatory process in Parkinson's disease: role for cytokines. Current Pharmaceutical Design, 11(8), 999-1016. doi: 10.2174/1381612053381620
Parameswaran, N., & Patial, S. (2010). Tumor necrosis factor-alpha signaling in macrophages. Critical Reviews in Eukaryotic Gene Expression, 20(2), 87-103. doi: 10.1615/critreveukargeneexpr.v20.i2.10
Shrestha, B., Zhang, B., Purtha, W.E., Klein, R.S., & Diamond, M.S. (2008). Tumor necrosis factor alpha protects against lethal West Nile virus infection by promoting trafficking of mononuclear leukocytes into the central nervous system. Journal of Virology, 82(18), 8956-8964. doi: 10.1128/JVI.01118-08
Swardfager, W., Lanctot, K., Rothenburg, L., Wong, A., Cappell, J., & Herrmann, N. (2010). A meta-analysis of cytokines in Alzheimer's disease. Biology Psychiatry, 68(10), 930-941. doi: 10.1016/j.biopsych.2010.06.012
Swaroop, J.J., Rajarajeswari, D., & Naidu, J.N. (2012). Association of TNF-alpha with insulin resistance in type 2 diabetes mellitus. Indian Journal of Medical Research, 135(1), 127-130. doi: 10.4103/0971-5916.93435
Tang, P., Hung, M.C., & Klostergaard, J. (1996). Human pro-tumor necrosis factor is a homotrimer. Biochemistry, 35, 8216-8225. doi: 10.1021/bi952182t
Wajant, H., Pfizenmaier, K., & Scheurich, P. (2003). Tumor necrosis factor signaling. Cell Death & Differentiation, 10, 45-65. doi: 10.1038/sj.cdd.4401189
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