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CD120a - TNFR1 - TNFR superfamily member 1A; CD120b - TNFR2 - TNFR superfamily member 1B; TNFR1 is the receptor type responsible for mediation of TNF-alpha induced sickness behavior, [3] and is involved in neurotoxic processes. [4] Elevated levels of TNFR1 has been found in severe mental disorders. [5]
7132 21937 Ensembl ENSG00000067182 ENSMUSG00000030341 UniProt P19438 P25118 RefSeq (mRNA) NM_001065 NM_001346091 NM_001346092 NM_011609 RefSeq (protein) NP_001056 NP_001333020 NP_001333021 NP_035739 Location (UCSC) Chr 12: 6.33 – 6.34 Mb Chr 6: 125.33 – 125.34 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Tumor necrosis factor receptor 1 (TNFR1), also known as tumor necrosis ...
The term death receptor refers to those members of the TNF receptor superfamily that contain a death domain, such as TNFR1, Fas receptor, DR4 and DR5. [4] They were named after the fact that they seemed to play an important role in apoptosis (programmed cell death), although they are now known to play other roles as well. [5]
CD120a: Tumor necrosis factor receptor superfamily member 1A (TNFR1), encoded by TNFRSF1A gene. Familial hibernian fever is caused by mutations in this gene. CD120b: Tumor necrosis factor receptor superfamily member 1B (TNFR2), encoded by TNFRSF1B gene. Constituent of the drug Enbrel, used to treat rheumatoid arthritis. CD121a
When TNF binds to its receptors, tumor necrosis factor receptor 1 (TNFR1) and tumor necrosis factor receptor 2 (TNFR2), a pathway of signals is triggered within the target cell, resulting in an inflammatory response. sTNF can only activate TNFR1, whereas tmTNF can activate both TNFR1 and TNFR2, [6] as well as trigger inflammatory signaling ...
Another motility-related mechanism was described: the failure of MCP-1 receptor (CCR2, CD192), TNF receptor 1 (TNFR1, CD120a), and TNF receptor 2 (TNFR2, CD120b) on the monocytes after exposure to pathophysiological concentrations (10 µM) of 4-HNE or after the phagocytosis of malarial pigment hemozoin. [44]
[5] [6] Like its counterpart, tumor necrosis factor receptor 1 (TNFR1), the extracellular region of TNFR2 consists of four cysteine-rich domains which allow for binding to TNFα. [ 7 ] [ 8 ] TNFR1 and TNFR2 possess different functions when bound to TNFα due to differences in their intracellular structures, such as TNFR2 lacking a death domain ...
Individuals with TRAPS have a mutation in the tumor necrosis factor receptor-1 (TNFR1) gene; [11] the mechanisms by which mutations in TNFR1 lead to the TRAPS phenotype are still unknown. Impaired shedding of the TNF receptor is one of the possible defects, most mutations affect the extracellular domain of the receptor, some also the cleavage site.