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

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

Death receptors play a significant position in directing apoptosis in mammalian cells. This means of energetic mobile dying is critical for a couple of organic strategies, e.g. for the law of the immune method. dying receptors are mobile floor receptors that transmit apoptotic signs initiated by means of corresponding dying ligands. Many advanced signaling pathways are activated and apoptosis is the ultimate results of a posh biochemical cascade of events.

Besides their position within the induction of telephone demise, proof now exists that loss of life receptors may be able to turn on a number of non-apoptotic signaling pathways which, reckoning on mobile context, could lead on to apoptosis resistance, secretion of pro-inflammatory proteins, proliferation and invasive progress of melanoma cells.

This publication seems to be on the molecular foundation of loss of life receptor signaling and the function of loss of life receptors in melanoma development.

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CD4 stimulation enhances signaling by the TCR by inducing aggregation of lipid rafts and formation of molecular assemblies at the site of the immunological synapse. During TCR activa- 30 M. Ramaswamy et al. tion, many of the cytoplasmic signaling proteins become detergent-insoluble, probably because of the association with lipid rafts (Kabouridis 2006; Viola et al. 1999). Studies have shown that monomeric TCR complexes have weak raft affinity compared to receptor crosslinking, which increases raft-associated TCR molecules and the amount of TCR found in detergent-insoluble raft domains.

However, despite expression of Fas on thymocytes and the susceptibility of most thymocytes to Fas-induced apoptosis, negative selection does not appear to depend on Fas–FasL interactions, since self-reactive T cells are deleted effectively in the thymus of both lpr and gld mice (Singer and Abbas 1994). Rather, Fas participates in the elimination of self-reactive T cells by a process known as restimulation induced cell death (RICD), an important ‘safety net’ for maintaining self-tolerance in T cells that have escaped central thymic tolerance.

2007). Palmitoylation of Fas is essential for raft association, and the apparent difference in raft-associated Fas observed in Type I-like vs. Type II-like cells could be due to the differential ability of the receptor to be palmitoylated. Interestingly, the death domain of TNFR1 is required for targeting to rafts, as deletion of the domain prevented the receptor from targeting to lipid rafts and resulted in more uniform distribution across the plasma membrane (Cottin et al. 2002). It is quite evident that posttranslational palmitoylation of Fas, allowing translocation to the lipid raft microdomains, is important for effective signaling.

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