By Harald Wajant (auth.), Holger Kalthoff (eds.)

Death receptors play a vital function in directing apoptosis in mammalian cells. This technique of energetic mobile dying is critical for a few organic techniques, e.g. for the rules of the immune process. demise receptors are cellphone floor receptors that transmit apoptotic signs initiated via corresponding demise ligands. Many complicated signaling pathways are activated and apoptosis is the ultimate results of a posh biochemical cascade of events.

Besides their position within the induction of mobilephone dying, facts now exists that demise receptors may be able to turn on numerous non-apoptotic signaling pathways which, looking on mobile context, could lead to apoptosis resistance, secretion of pro-inflammatory proteins, proliferation and invasive progress of melanoma cells.

This ebook appears on the molecular foundation of dying receptor signaling and the position of demise receptors in melanoma development.

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1997). From the crystal structures of TNF ligands bound to their receptors, it was found that TNF ligands exist in trimers. The stoichiometry of ligand-receptor complexes was 3:3, and trimeric structures have also been found for adaptor molecules downstream of the receptor (Bodmer et al. 2002). This supported a model of signaling where there is cooperativity and dissemination of signaling via formation of ligand:receptor:adaptor heterocomplexes. It was therefore not surprising that in patients with Type1A ALPS, where heterozygous mutations of the Fas receptor are localized mostly to the DD, lymphocytes were highly resistant to Fas-mediated apoptosis, even though they have an equal gene dosage of wild-type and mutant Fas genes.

This preassociation of Fas with lipid rafts in Type I cells allows them to undergo apoptosis even in the presence of low-valency Fas stimuli, while Type II cells cannot. Disruption of the lipid rafts through cholesterol chelation restores a requirement for Fascrosslinking in Type I cells, while having no effect on Type II cells (Muppidi and Siegel 2004). In mouse thymocytes, Fas recruitment and localization in the lipid rafts was critical for efficient DISC formation and subsequent cell death (Hueber et al.

1998). Interestingly, varying signaling thresholds for the apoptotic pathway appear to determine activation of alternate Fas signaling pathways. In ALPS patients with DD mutations, NF–kB signaling is activated in spite of the dominant interference caused by mutant receptors (Legembre et al. 2004). Biochemically, internalization of the Fas receptor induces the apoptotic pathway; however noninternalized receptors result in activation of NF–kB (Lee et al. 2006). Furthermore, in Fas resistant tumor cells, induction of NF–kB as well as activation of MAPK pathways increases motility and invasiveness, specifically in response to Fas crosslinking, but not to TNF-a or TRAIL treatment (Barnhart et al.

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Death Receptors and Cognate Ligands in Cancer by Harald Wajant (auth.), Holger Kalthoff (eds.)
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