Activation of Interferon-γ Inducing Factor Mediated by Interleukin-1β Converting Enzyme

Gu, Yun; Kuida, Keisuke; Tsutsui, Hiroko; Ku, George; Hsiao, Kathy; Fleming, Mark; Hayashi, Nobuki; Higashino, Kazuya; Okamura, Haruki; Nakanishi, Kenji; Kurimoto, Masashi; Tanimoto, Tadao; Flavell, Richard A.; Sato, Vicki L.; Harding, Matthew W.; Livingston, David J.; Su, Michael

doi:10.1126/science.275.5297.206

Cited by 1,087 publications

(780 citation statements)

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“…Other caspases, particularly those cleaving intracellular proteins associated with apoptosis, were at least 100-fold less active than caspase-1. 9 Similar studies with IL-18-deficient mice revealed its role in NK cell activity and cytokine induction. 12 A caspase-1-independent pathway of IL-18 secretion from FasL-stimulated macrophages was recently demonstrated, suggesting that FasL may induce alternative mechanisms for production of IL-18.…”

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confidence: 79%

“…Injection of P. acnes into caspase-1-deficient mice, followed by LPS challenge resulted in low levels of circulating IFNcompared with wild-type mice. [8][9][10][11] Injection of IL-18 restored the IFN-production in response to LPS in the caspase-1-deficient mice, 9 further supporting the concept that caspase-1 is involved in the production of active IL-18. Other caspases, particularly those cleaving intracellular proteins associated with apoptosis, were at least 100-fold less active than caspase-1.…”

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confidence: 84%

“…The resulting mature cytokines are subsequently released from the cell. 8,9 Studies in caspase-1-deficient mice demonstrated the important role of mature IL-18 as an inducer of IFN-and Th 1 responses. Injection of P. acnes into caspase-1-deficient mice, followed by LPS challenge resulted in low levels of circulating IFNcompared with wild-type mice.…”

Section: Academic Pressmentioning

confidence: 99%

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Production of a Biologically Active Human Interleukin 18 Requires Its Prior Synthesis as Pro-Il-18

et al. 2000

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confidence: 79%

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confidence: 84%

Section: Academic Pressmentioning

confidence: 99%

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Production of a Biologically Active Human Interleukin 18 Requires Its Prior Synthesis as Pro-Il-18

et al. 2000

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“…[12][13][14][15] These mice have a defect in the maturation of proIL-1b and proIL-18 and are resistant to the lethal effect of endotoxins. IL-18 was first described as an endotoxininduced factor that stimulates the production of interferon-g by splenocytes.…”

Section: Caspase-1 and It Substrate Il-1bmentioning

confidence: 99%

Inflammatory caspases and inflammasomes: master switches of inflammation

2006

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Fifteen years have passed since the cloning and characterization of the interleukin-1b-converting enzyme (ICE/caspase-1), the first identified member of a family of proteases currently known as caspases. Caspase-1 is the prototypical member of a subclass of caspases involved in cytokine maturation termed inflammatory caspases that also include caspase-4 caspase -5, caspase -11 and caspase -12. Efforts to elucidate the molecular mechanisms involved in the activation of these proteases have uncovered an important role for the NLR family members, NALPs, NAIP and IPAF. These proteins promote the assembly of multiprotein complexes termed inflammasomes, which are required for activation of inflammatory caspases. This article will review some evolutionary aspects, biochemical evidences and genetic studies, underlining the role of inflammasomes and inflammatory caspases in innate immunity against pathogens, autoinflammatory syndromes and in the biology of reproduction. Inflammatory CaspasesThe history of caspases began with the identification of an aspartate-specific protease activity involved in the conversion of the 31 kDa proIL-1b precursor to its active 17 kDa biologically active form, 1,2 and the identification of caspase-1 as the protease responsible for proIL-1b maturation. 3,4 The subsequent discovery of ced-3, that shares similarities with caspase-1 and which is involved in programmed cell death (PCD) in Caenorhabditis elegans, suggested that caspases might play fundamental roles in apoptosis. 5 As reviewed in the papers accompanying this issue of Cell Death and Differentiation, the role of apoptotic caspases in C. elegans and in vertebrates is crucial and deal with many facets of cell biology, development and diseases. In this review, we will focus on a subset of caspases present only in vertebrates and known as inflammatory caspases.Inflammatory caspases (also known as group I caspases) are encoded by three main genes in humans caspase-1, caspase-4 and caspase-5 and three main genes in mouse, caspase-1, caspase-11 and caspase-12. 6,7 In mammals, these caspases are characterized by the presence of a CARD domain at the N-terminus (Figure 1a). Human, chimp and mouse inflammatory caspases share significant similarity and are organized in a single locus (Figure 1c). Phylogenetic analysis of the conserved CARD domain suggests that the inflammatory caspases can be separated in evolutionaryrelated clusters (Figure 1b). The caspase-1 cluster contains caspase-1 and four other genes encoding decoy caspases: cop, inca1, inca2 and iceberg. These decoy caspase-1-like genes are absent in the mouse genome, suggesting that they have arisen recently by duplication of caspase-1. Although human and mouse caspase-1 are likely orthologues, sequence analysis suggests that human caspase-4 and caspase-5 have originated from a duplication of caspase-11. 7 However, the human caspase-12 gene, which in the chimp genome contains an SHG box important for it enzymatic activity, 8 evolved towards an enzymatically inactive form at some stage...

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“…13 It has been reported that other proteases are able to cleave IL-18 to inactive forms: caspase-3 acts on both proand mature IL-18, thereby generating a biologically inactive molecule of 14 kDa. 14 In previous studies, it has been proposed that both IL-18 and caspase-1 are produced by normal colon epithelium, where IL-18 may be involved in the regulation of the local immune response through IFN-␥ induction. By contrast, caspase-1 was no longer expressed in colon carcinoma, suggesting that the disappearance of mature IL-18 is associated with tumor progression in human colon cancer.…”

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Expression of interleukin‐18 in human ovarian carcinoma and normal ovarian epithelium: Evidence for defective processing in tumor cells

Wang

Gaggero

Rubartelli

et al. 2002

Intl Journal of Cancer

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Activation of Interferon-γ Inducing Factor Mediated by Interleukin-1β Converting Enzyme

Cited by 1,087 publications

References 26 publications

Production of a Biologically Active Human Interleukin 18 Requires Its Prior Synthesis as Pro-Il-18

Production of a Biologically Active Human Interleukin 18 Requires Its Prior Synthesis as Pro-Il-18

Inflammatory caspases and inflammasomes: master switches of inflammation

Expression of interleukin‐18 in human ovarian carcinoma and normal ovarian epithelium: Evidence for defective processing in tumor cells

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