Latest research on TNF-R2

Dimeric fusion protein consisting of the extracellular ligand-binding portion of the human 75 kilodalton (p75) tumor necrosis factor receptor (TNFR) linked to the Fc portion of human IgG1. The Fc component of etanercept contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. Etanercept is produced by recombinant DNA technology in a Chinese hamster ovary (CHO) mammalian cell expression system. It consists of 934 amino acids

Latest findings

Human ECs, like most other cell types, express two different TNFRs, designated TNFR1 (CD120a) and TNFR2 (CD120b) [19]. [source, 2002]
The success of antiTNF therapy of rheumatoid arthritis with infliximab (Remicade) and etanercept (Enbrel) has prompted us to seek other ways of inhibiting TNF production, and to seek to determine the cellular and molecular mechanisms underlying the excess and prolonged TNF synthesis in RA. [source, 2001]
In contrast to FasL, TNF-α activates two receptors, TNF-R1 and TNF-R2 (Baker and Reddy, 1998; Ashkenazi and Dixit, 1999), which promote cell proliferation after TRADD-mediated binding to an appropriate member of the TRAF family. [source, 2001]
However, in cells sensitized with CHX or Actinomycin D (Act D), oligomerized TNF-R1, but not TNF-R2 which lacks the death domain, can lead to apoptosis after binding to TRADD, which recruits FADD to activate the caspase pathway (Chinnaiyan et al., 1996; Hsu et al., 1996). [source, 2001]
TNF-α was tested in the concentration range of 0.02–0.5 nM to evaluate the impact of LXA4 and LXA4 analogs on the distinct signal transduction pathways of the TNF receptors CD120a (Kd 0.5 nM) and CD120b (Kd 0.1 nM) (34–36). [source, 1998]
These results indicate that LXA4 stable analogs are potent inhibitors of TNF-α–induced IL-8 release by intestinal epithelial cells and appear to selectively inhibit signals transduced via the CD120b TNF receptor (35, 36). [source, 1998]
The stable LXA4 analogs 15R/S-methyl-LXA4 and 16-phenoxy-LXA4 proved to be potent inhibitors of IL-8 release induced by the high affinity (CD120b) TNF-α receptor (Fig. 2), attenuating IL-8 release by as much as 62 ± 14% and 82 ± 11%, respectively. [source, 1998]
The fact that the majority of the TRAF2 and TRAF3 was lost from the cell after addition of ligand has implications for signaling via the other members of the TNF-R family, which also bind TRAF2 (i.e., TNF-R2, LT-βR, and CD30) or TRAF3 (CD30 and LT-βR). [source, 1997]
By analogy to studies with TNF-R2 (24), it may be that upon stimulation with CD154, CD40 oligomerizes and creates a higher affinity binding site for the TRAF molecules than found on Tank/I-TRAF. [source, 1997]
Recombinant human TNF-α with R32W and S86T substitutions (TNF-R1 specific) and TNF-α with D143N and A145R substitutions (TNF-R2 specific) were provided by Drs. [source, 1996]