By Harald Wajant (auth.), Holger Kalthoff (eds.)
Death receptors play a primary position in directing apoptosis in mammalian cells. This means of lively cellphone dying is critical for a few organic approaches, e.g. for the law of the immune process. dying receptors are cellphone floor receptors that transmit apoptotic indications initiated by way 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 cellphone demise, proof now exists that loss of life receptors may be able to turn on numerous non-apoptotic signaling pathways which, reckoning on mobile context, could lead on to apoptosis resistance, secretion of pro-inflammatory proteins, proliferation and invasive development of melanoma cells.
This e-book seems to be on the molecular foundation of loss of life receptor signaling and the position of loss of life receptors in melanoma development.
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Additional resources for Death Receptors and Cognate Ligands in Cancer
Receptor internalization is both actin and caspase dependent, indicating a feed-forward mechanism by which caspase-8 activity can enhance its own cleavage. The internalized receptor is then targeted to an endosomal pathway, since it colocalizes with the transferrin receptor (Algeciras-Schimnich et al. 2002). Internalization and capping occur more rapidly and prominently in Type I cells which correlates with more rapid DISC activation (Algeciras-Schimnich and Peter 2003; Eramo et al. 2004; Siegel et al.
In one instance, cell death is promoted through dissolution of receptor-associated signaling (TNFR1), while in another apoptosis is abrogated due to inefficient formation 32 M. Ramaswamy et al. of a signaling complex (Fas). As a result, lipid raft associated signaling has two very distinct outcomes in TNFR1 and Fas. Fas signaling should be seen as more of a dynamic process that involves more than just ligand binding to receptor, and that which also takes into account local microenvironment, subcellular localization, secondary modifications of Fas and global cell signaling pathways.
S-palmitoylation is a reversible modification involving addition of a 16-carbon palmitate moiety to a cysteine residue via a thioester linkage, and can be readily cleaved by palmitoyl thioesterases. An interesting feature of S-palmitoylation is its dynamic nature: cycles of palmitoylation and depalmitoylation occur in a regulated fashion for many proteins, allowing for translocation in and out of lipid raft microdomains (Resh 2006). Fas is palmitoylated at cysteine 199, just proximal to the cytoplasmic juxamembrane region (Chakrabandhu et al.