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Hypermethylation of the proapoptotic genes BCL2 L11 (show BCL2L11 Proteins) and TNFRSF25 is observed in pleomorphic adenoma of the salivary glands. However, this phenomenon did not impact mRNA transcription.
the DR3/TL1A (show TNFSF15 Proteins) pathway directly enhances human OC formation and resorptive activity, controlling expression and activation of CCL3 (show CCL3 Proteins) and MMP-9 (show MMP9 Proteins).
Untreated children with IBD have higher percentage of DR3(+) PBMCs.
In addition to apoptosis, DR3 can robustly trigger necroptotic cell death and provide evidence for TL1A (show TNFSF15 Proteins)-induced, DR3-mediated necrosome assembly. DR3-mediated necroptosis critically depends on receptor-interacting protein 1 (RIP1 (show RIPK1 Proteins)) and RIP3 (show RIPK3 Proteins), the core components of the necroptotic machinery, which activate the pseudo-kinase mixed lineage kinase domain-like, the prototypic downstream effector molecule of necroptosis.
Data suggest that human regulatory T-lymphocytes express DR3 and demonstrate DR3/TL1A (show TNFSF15 Proteins)-mediated activation of signaling via MAP kinases and NFkappaB (show NFKB1 Proteins). (DR3 = death receptor 3; TL1A/TNFSF15 (show TNFSF15 Proteins) = tumor necrosis factor (show TNF Proteins) [ligand] superfamily, member 15)
These results raise the possibility for involvement of TL1A (show TNFSF15 Proteins)/DR3/DR3-mediated mechanisms in epithelial-mesenchymal interactions and the development of inflammation-induced intestinal fibrosis in Crohn's disease.
Activation of DR3 is accompanied by inhibition of apoptosis of naive T-lymphocytes in children with acute infectious mononucleosis.
Biologics beyond TNF-alpha (show TNF Proteins) inhibitors and the effect of targeting the homologues TL1A (show TNFSF15 Proteins)-DR3 pathway in chronic inflammatory disorders.
Higher DR3 levels were associated with early stage chronic lymphocytic leukemia.
DR3 is efficiently activated by soluble TL1A (show TNFSF15 Proteins) trimers.
in vivo targeting of the TNF (show TNF Proteins) superfamily receptor TNFRSF25 using the TL1A (show TNFSF15 Proteins)-Ig fusion protein, along with IL-2 (show IL2 Proteins), resulted in transient but massive Treg expansion in donor mice; transplantation of Treg-expanded donor cells facilitated transplant tolerance without GVHD, with complete sparing of graft-versus-malignancy.
This work describes both a novel function and essential requirement for the DR3/TL1A (show TNFSF15 Proteins) pathway in acute, resolving, and chronic inflammation in the peritoneal cavity.
this study shows that DR3 signaling protects mice from acute dextran sodium sulfate colitis because DR3-/- mice showed more severe mucosal inflammation and increased mortality
the critical effect of the state of T-cell activation on clinical outcomes after activation of DR3, is reported.
These data identify new roles for DR3 in regulating OB-dependent bone mineral apposition.
Data indicate that death receptor 3 (DR3) depletion gives rise to an increased anti-apoptotic potential.
these data identify TL1A (show TNFSF15 Proteins)-DR3 interactions as a novel pathway that promotes Th9 differentiation and pathogenicity. TL1A (show TNFSF15 Proteins) may be a potential therapeutic target in diseases dependent on IL-9 (show IL9 Proteins).
TL1A (show TNFSF15 Proteins) induces NF-kappaB (show NFKB1 Proteins) activation in EC in renal and cardiac tissue from wild type but not DR3 knock-out mice.
Both in supernatant and as purified fusion protein, TL1A (show TNFSF15 Proteins)-Ig binds to TNFRSF25 transfected--but not untransfected--P815 tumor cells as determined by flow cytometry.
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is expressed preferentially in the tissues enriched in lymphocytes, and it may play a role in regulating lymphocyte homeostasis. This receptor has been shown to stimulate NF-kappa B activity and regulate cell apoptosis. The signal transduction of this receptor is mediated by various death domain containing adaptor proteins. Knockout studies in mice suggested the role of this gene in the removal of self-reactive T cells in the thymus. Multiple alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported, most of which are potentially secreted molecules. The alternative splicing of this gene in B and T cells encounters a programmed change upon T-cell activation, which predominantly produces full-length, membrane bound isoforms, and is thought to be involved in controlling lymphocyte proliferation induced by T-cell activation.
apoptosis inducing receptor
, apoptosis-inducing receptor AIR
, apoptosis-mediating receptor DR3
, apoptosis-mediating receptor TRAMP
, death domain receptor 3 soluble form
, death receptor beta
, lymphocyte-associated receptor of death
, protein WSL-1
, tumor necrosis factor receptor superfamily member 25
, tumor necrosis factor receptor superfamily, member 12 (translocating chain-association membrane protein)
, tumor necrosis factor receptor superfamily, member 12
, tumor necrosis factor receptor superfamily, member 25
, translocating chain-association membrane protein
, tumor necrosis factor receptor superfamily, member12