cFLIPCellular FLICE-Like Inhibitory Protein
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mRNA levels of IL-1[beta] (a), IL-6 (b), IL-8 (c), IL-1[micro] (d), IL- 17a (e), TNF-[alpha] (f), TNFR (g), IFN[gamma] (h), CXCL-11 (i), iNOS (j), COX-2 (k), and cFLIP (l) were detected by real-time RT-PCR.
Nakano, "FLIP the switch: regulation of apoptosis and necroptosis by cFLIP," International Journal of Molecular Sciences, vol.
Cellular FLICE-inhibitory protein (cFLIP) isoforms block CD95- and TRAIL death receptor-induced gene induction irrespective of processing of caspase-8 or cFLIP in the death-inducing signaling complex.
The study analyzed the role of cFLIP in breast cancer cells' resistance to TRAIL-induced apoptosis.
Such conclusion was drawn from the evidence that the inhibition of their expression through treatments with Doxorubicin (anthracycline, widely used in chemotherapy) or with SAHA (Histone deacetylases inhibitor), as well as the silencing of its expression through cFLIP siRNA oligos (small interfering RNA), resulted in the sensitisation of breast cancer cells to TRAIL-induced apoptosis.
p53 upregulates cFLIP, inhibits transcription of NF-[kappa]B-regulated genes and induces caspase-8-independent cell death in DLD-1 cells.
Kim et al., "Increased hepatic fibrosis and JNK2-dependent liver injury in mice exhibiting hepatocyte-specific deletion of cFLIP," American Journal of Physiology - Gastrointestinal and Liver Physiology, vol.
However, the effects of alantolactone on NF-[kappa]B target genes, including IAP1, IAP2, XIAP, cFLIP, survivin, and TRAF1, have not been elucidated yet, while isoalantolactone is not reported yet to affect nuclear factor [kappa]B (NF-[kappa]B) signaling.
The interaction of the TNFR-1 with either FADD or pro-caspase-8 and -10, via both death domain (DD) and death effector domain (DED) triggers the apoptotic signaling cascade, whereas the interaction with negative regulator cFLIP (FADD-like IL-1[beta]-converting enzyme-inhibitory protein) will block this apoptotic signaling cascade, leading to cellular survival and NF-[kappa]B-mediated proinflammatory response (Figure 4).
The activation of caspase-8 at the DISC can be potently regulated by cellular FLICE-like inhibitory protein (cFLIP).