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Details on Person TLR3 and TLR4 were shown to mediate apoptosis in various hum...
| Class:Id | Summation:9013892 |
|---|---|
| _displayName | TLR3 and TLR4 were shown to mediate apoptosis in various hum... |
| _timestamp | 2017-07-26 06:02:18 |
| created | [InstanceEdit:9013896] Shamovsky, Veronica, 2017-07-26 |
| text | TLR3 and TLR4 were shown to mediate apoptosis in various human cell lines in the FADD:caspasse-8-dependent manner (Kalai M et al. 2002; Kaiser WJ and Offermann MK 2005; Estornes Y et al. 2012). Caspase-8 zymogens (procaspase-8) are present in the cells as inactive monomers, containing a large N-terminal prodomain with two death effector domains (DED), and a C-terminal catalytic subunit composed of small and a large domains separated by a smaller linker region (Donepudi M et al. 2003; Keller N et al. 2009). Dimerization is required for caspase-8 activation (Donepudi M et al. 2003). The dimerization event occurs at the receptor signaling complex. Once dimerized, caspase-8 zymogen undergoes a series of autoproteolytic cleavage events at aspartic acid residues in their interdomain linker regions. A second cleavage event between the the N-terminal prodomain and the catalytic domain releases the active caspase from the activation complex into the cytosol. The resulting fully active enzyme is a homodimer of catalytic domains, where each domain is compsed of a large p18 and a small p10 subunit (Keller N et al. 2009; Oberst A et al. 2010). |
| (summation) | [Reaction:9013895] Caspase-8 processing within TLR3 complex [Homo sapiens] |
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