Status
Please wait ...

Details for receptor: TNFR1

  • Top
  • General information
  • Subunits
    •
  • External resources
  • General information
  • Hormones
  • Anatomical structures
  • Click to access the toolbox
EndoNet ID: ENR00717

To link to the content of EndoNet use the EndoNet ID that is given on the detail pages in the format ENX0000, where X is a place holder for the type of the component (e. g. R for receptor or C for anatomical structure).
As URL for the linking append this ID to the detail page for this type of component.
For an hormone that would be: 

http://endonet.bioinf.med.uni-goettingen.de/hormone/ENH00000

It is also possible to use the search of EndoNet to link to the right detail page. The URL should look like 

http://endonet.bioinf.med.uni-goettingen.de/search/ENC00000
If the search pattern is unambigious the user is directed to the corresponding detail page.

Synonyms

  • TNFR1
  • TNFRSF1A
  • TNF-R1
  • TNF-RI
  • tumor necrosis factor receptor 1
  • TNFAR
  • p55 TNF receptor
  • TNF-R55
  • p55-R
  • p55TNFR
  • p55
  • TNFR60

General information

  • The majority of TNFR1 molecules are localized to the Golgi apparatus. [1]
  • The potent osteoclastogenic agent, tumor necrosis factor-alpha (TNF), exerts its biological effects via two receptors, namely TNF receptors 1 (p55r) and 2 (p75r), each present on osteoclast precursors. [2]
  • Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. [3]
  • Minimal TNF-R1 immunoreactivity in hepatocytes was observed in patients with AH and controls. [4]
  • The urinary TNF-binding proteins constitute soluble forms of the two molecular species of the cell surface TNF receptors. [5]
  • The cDNA for the type I TNF-R encodes both the cell surface and a soluble form of the receptor. [6]
  • Ligand-activated TNFR1 promotes the activation of the transcription factor nuclear factor-κB (NF-κB) via recruitment of TNFR associated death domain (TRADD) protein, receptor-interacting protein‑1 (RIP1) and TNFR-associated protein‑2 (TRAF2) at the cell surface. [7]
  • ubiquitously expressed [8]

Links to other resources

UniProt P19438
Ensembl ENST00000440083

Subunit information

membrane form

Sequence 
IYPSGVIGL VPHLGDREK RDSVCPQGK 
YIHPQNNSI CCTKCHKGT YLYNDCPGP 
GQDTDCREC ESGSFTASE NHLRHCLSC 
SKCRKEMGQ VEISSCTVD RDTVCGCRK 
NQYRHYWSE NLFQCFNCS LCLNGTVHL 
SCQEKQNTV CTCHAGFFL RENECVSCS 
NCKKSLECT KLCLPQIEN VKGTEDSGT 
TVLLPLVIF FGLCLLSLL FIGLMYRYQ 
RWKSKLYSI VCGKSTPEK EGELEGTTT 
KPLAPNPSF SPTPGFTPT LGFSPVPSS 
TFTSSSTYT PGDCPNFAA PRREVAPPY 
QGADPILAT ALASDPIPN PLQKWEDSA 
HKPQSLDTD DPATLYAVV ENVPPLRWK 
EFVRRLGLS DHEIDRLEL QNGRCLREA 
QYSMLATWR RRTPRREAT LELLGRVLR 
DMDLLGCLE DIEEALCGP AALPPAPSL 
LR

Binding hormones

  • TNF-alpha
    • Tumor necrosis factor (TNF) activates pro-inflammatory functions of vascular endothelial cells (EC) through binding to receptor type 1 (TNFR1) molecules expressed on the cell surface. [1]
  • TNF-beta
    • TNF-beta in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM. [3]

Anatomical structures with this receptor

  • bronchial_epithelial_cell

    Influences

    • positive IL-8

  • osteoclast

  • pneumocyte_type_II

    Influences

    • positive IL-8

  • Kupffer_cell_stellate_cell_of_liver

  • hepatocyte

    Influences

    • positive TGF-alpha
      • In primary hepatocyte cultures, TNF not only potentiates growth factor-stimulated proliferation, but acts as a mitogen itself through the induced release of autocrine transforming growth factor- (TGF-) and its activation of serine-threonine protein kinase B (PKB)/Akt and extracellular signal-regulated kinase (ERK). [9]
    • positive IL-1 alpha
      • Induced IL-1alpha release from hepatocyte is contingent on both TNF and autocrine TGF-alpha. [9]
    • positive IL-1 beta
      • Induced IL-1alpha release from hepatocyte is contingent on both TNF and autocrine TGF-alpha. [9]
    • positive IL-1RA
      • TNF induces the release of IL-1ra. [9]

    Induced phenotypes

    • antagonizing IL-1alpha/beta ligand activity
      • TNF induces the release of IL-1ra, which antagonizes IL-1alpha/beta ligand activity. [9]
    • positive regulation of apoptosis
      • TNF-induced autocrine TGF- and IL-1alpha/beta contribute to multiple intracellular signaling pathways that govern hepatocyte apoptosis. [9]
      • Autocrine IL-1alpha/beta regulates proapoptotic signaling through JNK and p38 pathways. [9]
    • positive regulation of cell proliferation
      • TNF-induced autocrine TGF- and IL-1alpha/beta contribute to multiple intracellular signaling pathways that govern hepatocyte proliferation. [9]
      • 101 Autocrine TGF-alpha regulates pro-proliferative/antiapoptotic signaling through the ERK and, in the absence of Adenoviral infection, Akt pathways. 2452 [10]

  • dendritic_cell_in_lymphoid_tissues_follicular

  • macrophage

    Influences

    • positive PAF
      • TNF induce PAF synthesis by monocyte/macrophages. [11]

  • monocyte

    Influences

    • positive PAF
      • TNF induce PAF synthesis by monocyte/macrophages. [11]

  • neutrophil_granulocyte

    Influences

    • positive IL-8
      • Early TNF-alpha (accumulating 4 hrs after LTA exposure), considerably stimulated the late phase of IL-8 secretion in an autocrine manner. [12]

  • stromal_fibroblast

  • epithelial_cell_with_microvilli

    Influences

    • positive eotaxin
    • positive IL-8

  • epithelial_cell

  • bone_marrow

    Induced phenotypes

    • atherosclerosis
      • In atherosclerosis, TNF considered to promote plaque growth and progression. [13]
      • Bone-marrow derived p55 TNFR promotes atherosclerosis development by enhancing lesional foam-cell formation and by promoting expression of pro-atherosclerotic chemokines, like MCP-1. [14]

  • lipocyte_of_liver

    Influences

    • positive RANTES
      • Hepatic stellate cells secrete RANTES after stimulation with TNF-alpha, IL-1beta, and CD40L in an inhibitor-kappaB (I kappa B)kinase (IKK)2/NF kappaB- and JNK-dependent manner. [15]

  • adipose_tissue

    Influences

    • positive leptin
      • Leptin secretion is regulated by TNF-alpha posttranslationally. This secretagogue-like activity is consistent with the existence of regulatable pools of leptin and may contribute in part to the insulin resistance properties of TNF-alpha as well as the adipostatic mechanisms of leptin. [16]
    • negative insulin
      • TNF alpha regulates leptin release from adipocztes, therebz influencing insulin secretion. [16]
      • The ability of leptin and TNF/alpha to suppress insulin secretion from the pancreas beta cells might also contribute to the abnormalities in glucose homeostasis in obesity. [16]

    Induced phenotypes

    • negative regulation of insulin receptor signaling pathway
      • TNF-alpha inhibits insulin receptor signaling in cultured cells. [16]
      • TNF-α inhibits insulin signaling via stimulation of p55 TNFR and sphingomyelinase activity, which results in the production of an inhibitory form of insulin receptor substrate-1 . [17]
    • regulation of glucose homeostasis
      • The ability of TNF-alpha to regulate insulin secretion from the pancreatic beta cells might contribute to the abnormalities in glucose homeostasis in obesity . [16]
    • hyperinsulinemia
      • The obesity-related increase in TNF-alpha production is positively correlates with hyperinsulinemia. [18]
    • insulin resistance
      • The obesity-related increase in TNF-alpha production positively correlates with increased insulin resistance. [18]
      • More direct measures of insulin sensitivity have indicated TNF alpha as potential mediator of insulin resistance in obesity. [18]
    • negative regulation of gene expression
      • TNF-alpha inhibits expression of the rate-limiting enzyme for long chain fatty acid synthesis, acetyl CoA carboxylase, in cultured adipocytes. [19]
    • obesity
      • TNF-alpha can act directly on adipocytes to regulate the release of a preformed pool of leptin. Elevated adipose tissue expression of TNF-alpha that occurs in obesity may contribute to obesity-related hyperleptinemia. [16]
      • Leptin secretion is regulatd by TNF-alpha posttranslationally. This secretagogue-like activity is consistent with the existence of regulatable pools of leptin and may contribute in part to the insulin resistance properties of TNF-alpha as well as the adipostatic mechanisms of leptin. [16]
Reference