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Facts about Tumor necrosis factor receptor superfamily member 1B.
This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 cubes TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity.
Human | |
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Gene Name: | TNFRSF1B |
Uniprot: | P20333 |
Entrez: | 7133 |
Belongs to: |
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No superfamily |
CD120b antigen; CD120b; Etanercept; p75 TNF receptor; p75TBPII; p75TNFR; soluble TNFR1B variant 1; TNF RII; TNFBRp80 TNF-alpha receptor; TNF-R2; TNFR2TNFR1B; TNF-R75; TNFR80; TNFRII; TNF-RII; TNF-R-II; TNFR-II; TNFRSF1B; tumor necrosis factor beta receptor; tumor necrosis factor binding protein 2; Tumor necrosis factor receptor 2; tumor necrosis factor receptor superfamily member 1B; tumor necrosis factor receptor superfamily, member 1B; Tumor necrosis factor receptor type II
Mass (kDA):
48.291 kDA
Human | |
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Location: | 1p36.22 |
Sequence: | 1; NC_000001.11 (12166948..12209222) |
[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.; [Tumor necrosis factor-binding protein 2]: Secreted.
Multifunctional proinflammatory cytokine TNFRSF1B is present in the muscles and joints. It's an abnormality in the musculoskeletal system as well as a tumor-associated TNF receptor. This article will outline the most effective applications of this marker. This article will give you an overview of the protein and its many roles. Find out more about how it can be utilized for research.
TNF-a is a part of the TNF family of proinflammatory cytokines. It functions through receptors and has been linked to the development of autoimmune diseases as well as insulin resistance. Knockout studies also suggest that this protein might have neuroprotective properties. Although it has yet to be defined TNF-a might contribute to neuroinflammation in the brain.
Neuroinflammation triggered by metabolic syndrome has been associated with the development of Alzheimer's disease and diabetes. Neuroinflammation can also lead to impaired insulin action in brain cells. TNF dysregulation is strongly linked to obesity and diabetes. TNF also causes carbohydrate dysregulation and hinders the action of insulin. It also enhances hepatic glucose generation and clearance of glucose.
TNF has a variety of endpoint actions, including metabolic reprograming of carbohydrates as well as amino acids, lipids, and lipids. It can also alter intracellular signalling networks, cytoskeletal modifications, and other endpoints. In the absence of any resolution to inflammation or prolonged stress, TNF's catabolic influence can be dangerous. In a subsequent paper, we will discuss this process.
TNF-a may also inhibit cardiac function and lead to heart failure. Studies have shown that TNF-a might be involved in myocardial injury as well as heart failure. Although susceptibility to genetic mutations may be linked to genetic characteristics but genetic studies of a specific gene's function in heart disease are still being conducted. The 6p21.3 region contains the genes that produce TNF-a.
TNF-a is linked to nonalcoholic steatohepatitis (NASH), cirrhosis and obesity. Increased TNF activity is associated with end-stage liver disease, including NASH. NASH progression is promoted by the liver-specific TNF in rodent models. TNF genotypes are related to susceptibility for colorectal liver metastasis in patients suffering from NAFLD.
TNF-a is produced as a prohormone substance that is tightly connected to the cell membrane of many cell types. It is processed to a mature protein containing 157 residues after the cleavage of a 76-residue signal protein. TNF-a was initially known as cachectin in the 1970s was first identified as necrosis factors. The protein is present in two bioactive forms: soluble TNF-a and transmembrane TNF-a that block the cytotoxic effects of TNF-a.
TNFRSF1B is a novel multifunctional proinflammatory cytokine , with a variety of functions. In humans, TNFRSF1B has two receptors, TNFR1 and TNFR2; TNF alpha and TNF beta connect to TNFR1 while TNF beta connects to a different cytokine receptor, TNFR2.
There are a number of genetic variants affecting the production of TNF, and they are associated with certain diseases, including malaria. Shin et al. Shin and colleagues. (2004) found that certain genetic variants associated with a 3.7-fold increase in mortality from all causes in patients suffering from Septic shock. These results suggest that TNFRSF1B is a key factor in malaria-related illnesses like septic shock.
TNF is involved in multiple ways in metabolic disorders and non-alcoholicfatty-liver disease. TNF activity is linked to end-stage liver disease and associated with increased levels of inflammation. Evidence suggests that hepatic TNF activation can trigger NASH progress in rodent models. Variations within the TNF genotype can make NAFLD patients more susceptible to colorectal metastases. The metabolic and obesity diseases could be connected, and reducing TNF activity in patients suffering from non-alcoholic fatty liver disease (NAFLD) can prevent diabetes.
While TNF is a multifunctional cytokine, its action is primarily controlled by membrane trafficking. The authors discovered the joint trafficking pathway which binds both actions. This may reduce the cost and increase the immune response. The research shows that TNFFA is transported through the vesicle-associated membrane protein-3 that is found in the Golgi. This protein then fuses with the cell surface receptor, which allows the rapid release of TNF alpha and expanding the membrane for phagocytosis.
TNF alpha is a cytokine with multiple functions belonging to the tumor necrosis factor superfamily. It is a member of the TNFR superfamily and is extensively secreted. It has a wide variety of biological effects. TNF alpha is an anti-cancer agent. It isn't clear if the protein is a potent anti-cancer agent.
TNFRSF1B is an abnormal gene that encodes for the tumor necrosis factor receptor 1 (TNFR1). This receptor is located on the cells' surface and is vital for the body to guard against infection. TNF receptor activation is caused by a defect in TNFR1 gene. The over-expression of this protein can trigger an inflammation response. Researchers believe that TRAPS is controlled by the gene. However, the exact mechanism of TRAPS development is still not identified.
TNFRSF1B has been linked with susceptibility to ankylosing spondylitis, which is a disease triggered by the presence of abnormal levels of TNF. This gene is crucial in the regulation of the immune system and is implicated in the pathogenesis ankylosing. TNF regulates its biological function by binding to cell surface receptors. TNFR1 is prone to developing abnormal conformational changes due to an genetic polymorphism. These changes can cause abnormal signalling. However, research at present isn't enough and controversial to establish an exact causal link between TNFR1B and AS.
The TNFRSF1B gene is located on the short arm of the chromosome 12 (chromosome 12p13.2). 46 pairs of chromosomes are found in the human body, ranging from one to 22. Males have one X and one Ychromosome while females have two. The chromosomes can also be divided into multiple bands. The short arm of chromosome 12 has been named 12p13.
Despite the plethora of evidence linking TNFR2 and TNFRSF1B levels with disease susceptibility only a few studies have looked into the impact of TNFRSF1B gene variant on the development of lupus. However, the increased activity of Treg cells in patients suffering from lupus who have two copies of VNTR could be due to higher numbers of Treg cells.
The TNF receptor is commonly expressed in cancer cells. The TNFRSF gene, which is the most abundant one, is among these cells. In addition to TNFRSF1B the gene contains GITR and OX40 and is a part of the fundamental Treg signature, which comprises the top 10 genes that are expressed by these cells. We discovered that TNFRSF1B was most often expressed by tumor infiltrating Tregs.
The TNFRSF1B gene has been identified in at least 25 types of cancers, including multiple myeloma and colon cancer. The presence of this gene could cause an increase in the growth of tumors. TNFRSF1B is also linked to Sezary syndrome, a rare illness characterized by high TNFR2 expression.
TNFRSF1B is part of the TNF superfamily, which comprises 19 structurally related cytokines. Although both possess TNF-binding motifs However, they differ in their intracellular domains. The death domain of TNFR1 interacts with an TNFR-associated death-domain protein. This entices other TNF receptor kinases (RIPK), CTLA4 and into a signaling complex called the signalosome. It is also a major target of apoptosis induced by TNF and inflammatory intestinal disease. These diseases are being treated with a variety of drugs.
P75 regulates angiogenesis in tumors, as does TNFRSF1B. TNF-mediated inhibition is more effective in tumors that are resistant than those with normal levels of the PLGF and p75. A recent study in mice carrying a p75KD mutation inhibited angiogenesis and tumor growth.
A recent study demonstrated that mTNF therapy can slow down the growth of breast cancer tumors the mouse model of breast cancer. The drug was also shown to cause complete regression of tumors. mTNFR-1a doesn't just inhibit TNF-a's expression but also inhibits expression of the adhesion molecule CD44v6. TNF-a's cytotoxicity is also increased by CD44v6.
The presence of TNFRSF1B in a tumor's cells surface is linked to better overall and non-disease-free survival. Furthermore, the detection of TNFRSF1B in tumor cells can assist in identifying patients who might benefit from treatment for anti-TNF. The study suggests that TNFRSF1B gene polymorphisms play an significant role in triggering CD.
PMID: 2172983 by Kohno T., et al. A second tumor necrosis factor receptor gene product can shed a naturally occurring tumor necrosis factor inhibitor.
PMID: 2160731 by Smith C.A., et al. A receptor for tumor necrosis factor defines an unusual family of cellular and viral proteins.
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