Abstract |
Death receptors belong to the tumor necrosis factor receptor superfamily and can induce apoptosis through activation of procaspase-8. The cellular FLICE-inhibitory protein (c-FLIP) is able to modulate activation of procaspase-8 and thereby prevents induction of apoptosis mediated by death receptors. As an important modulator of caspase-8, c-FLIP regulates life and death in various types of normal cells and tissues, such as lymphoid cells, and renders resistance to death receptor-mediated apoptosis in many types of cancer cells. In addition to an apoptosis modulator, c-FLIP has been shown to exert other physiological functions related to cell proliferation and tumorigenesis. Dysregulation of c-FLIP expression has been shown to be associated with various diseases, such as cancer and autoimmune diseases, and c-FLIP might be a critical target for therapeutic intervention. This review focuses on recent findings about the physiological function and intracellular regulation of c-FLIP.
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Authors | Takao Kataoka |
Journal | Critical reviews in immunology
(Crit Rev Immunol)
Vol. 25
Issue 1
Pg. 31-58
( 2005)
ISSN: 1040-8401 [Print] United States |
PMID | 15833082
(Publication Type: Journal Article, Review)
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Chemical References |
- CASP8 and FADD-Like Apoptosis Regulating Protein
- CFLAR protein, human
- Intracellular Signaling Peptides and Proteins
- Receptors, Tumor Necrosis Factor
- CASP8 protein, human
- Caspase 8
- Caspases
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Topics |
- Animals
- Apoptosis
(drug effects, immunology, physiology)
- CASP8 and FADD-Like Apoptosis Regulating Protein
- Caspase 8
- Caspases
(drug effects, immunology, physiology)
- Humans
- Intracellular Signaling Peptides and Proteins
(genetics, pharmacology, physiology)
- Receptors, Tumor Necrosis Factor
(antagonists & inhibitors, immunology, physiology)
- Signal Transduction
(immunology, physiology)
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