FLIP is an apoptosis regulator protein which functions as a crucial link between cell survival and cell death pathways in mammalian cells and acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. FLIP lacks enzymatic (caspase) activity. FLIP is highly expressed in skeletal muscle, pancreas, heart, kidney, placenta and peripheral blood leukocytes.
- The role of c-FLIP in modulation of CD95-induced apoptosis: S. Scaffidi, et al.; J. Biol. Chem. 274, 1541 (1999)
- An inducible pathway for degradation of FLIP protein sensitizes tumor cells to TRAIL-induced apoptosis: Y. Kim, et al.; J. Biol. Chem. 277, 22320 (2002)
- Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8: M.R. Sprick, et al.; EMBO J. 21, 4520 (2002)
- Enhancement of Apo2L/TRAIL (tumor necrosis factor-related apoptosis-inducing ligand)-induced apoptosis in non-small cell lung cancer cell lines by chemotherapeutic agents without correlation to the expression level of cellular protease: S. Frese, et al.; J. Thorac. Cardiovasc. Surg. 123, 168 (2002)
- Lack of Proapoptotic Activity of Soluble CD95 Ligand Is Due to Its Failure to Induce CD95 Oligomers: S. Jang, et al.; J. Int. Cyt. Res. 23, 441 (2003)
- Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation: M. Leverkus, et al.; Mol. Cell. Biol. 23, 777 (2003)
- Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice: S.T. Eichhorst, et al.; Nature Med. 10, 602 (2004)
- The c-FLIP-NH2 terminus (p22-FLIP) induces NF-kappaB activation: A. Golks, et al.; J. Exp. Med. 203, 1295 (2006)
- Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis: I.N. Lavrik, et al.; Blood 108, 559 (2006)
- The role of CAP3 in CD95 signaling: new insights into the mechanism of procaspase-8 activation: A. Golks, et al.; Cell Death Diff. 13, 489 (2006)
- Expression of c-FLIP is primarily detected in diffuse large B-cell lymphoma and Hodgkin's lymphoma and correlates with lack of caspase 8 activation: I.S. van Houdt, et al.; Histopathology 51, 778 (2007)
- CD95 Stimulation Results in the Formation of a Novel Death Effector Domain Protein-containing Complex: I.N. Lavrik, et al.; J. Biol. Chem. 283, 26401 (2008)
- A New C-terminal Cleavage Product of Procaspase-8, p30, Defines an Alternative Pathway of Procaspase-8 Activation: J.C. Hoffmann, et al.; Mol. Cell Biol. 29, 4431 (2009)
- Stoichiometry of the CD95 Death-Inducing Signaling Complex: Experimental and Modeling Evidence for a Death Effector Domain Chain Model: K. Schleich, et al.; Mol. Cell 47, 1 (2012)
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