Murine Caspase-11, an ICE-Interacting Protease, Is Essential for the Activation of ICE

Wang, Suyue; Miura, Masayuki; Jung, Yong‐Keun; Zhu, Hong; Li, En; Yuan, Junying

doi:10.1016/s0092-8674(00)80943-5

Cited by 650 publications

(630 citation statements)

References 33 publications

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“…The lack of CASP4, rather than CASP1, protects against lipopolysaccharide-induced septic shock due to reduced secretion of the pro-inflammatory cytokines IL1A and IL1B [15,40]. Yet, casp4 −/- mice are highly susceptible to infection with virulent B. pseudomallei and avirulent B. thailandensis resulting in increased mortality [18].…”

Section: Discussionmentioning

confidence: 99%

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CASP4/caspase-11 promotes autophagosome formation in response to bacterial infection

Krause¹,

Caution²,

Badr³

et al. 2018

Autophagy

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CASP4/caspase-11-dependent inflammasome activation is important for the clearance of various Gram-negative bacteria entering the host cytosol. Additionally, CASP4 modulates the actin cytoskeleton to promote the maturation of phagosomes harboring intracellular pathogens such as Legionella pneumophila but not those enclosing nonpathogenic bacteria. Nevertheless, this non-inflammatory role of CASP4 regarding the trafficking of vacuolar bacteria remains poorly understood. Macroautophagy/autophagy, a catabolic process within eukaryotic cells, is also implicated in the elimination of intracellular pathogens such as Burkholderia cenocepacia. Here we show that CASP4-deficient macrophages exhibit a defect in autophagosome formation in response to B. cenocepacia infection. The absence of CASP4 causes an accumulation of the small GTPase RAB7, reduced colocalization of B. cenocepacia with LC3 and acidic compartments accompanied by increased bacterial replication in vitro and in vivo. Together, our data reveal a novel role of CASP4 in regulating autophagy in response to B. cenocepacia infection.

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Section: Discussionmentioning

confidence: 99%

“…casp4 −/- /caspase-11 −/- mice were generously provided by Dr. Junying Yuan (Harvard Medical School, Boston, MA, USA) [40]. casp1 −/− Casp4/Casp-11Tg mice were a gift from Dr. Vishva Dixit (Genentech) [15].…”

Section: Methodsmentioning

confidence: 99%

CASP4/caspase-11 promotes autophagosome formation in response to bacterial infection

Krause¹,

Caution²,

Badr³

et al. 2018

Autophagy

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“…These mice fail to produce mature IL-1b and are resistant to endotoxic shock induced by bacterial endotoxins. 34 Moreover, caspase-11-deficient embryonic fibroblasts are resistant to apoptosis induced by ectopic expression of caspase-1, suggesting that caspase-11 is an upstream activator of caspase-1. 34 Unlike caspase-1, the expression of caspase-11 is LPS-inducible, and it is reasonable to postulate that other members of the family are regulated at the transcriptional or translational level by extracellular stimuli.…”

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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“…Caspase-1 activation needs to be maintained under tight regulation to control the magnitude of the inflammatory response, avoiding its deleterious effects, such as occurs in sepsis. Supporting this notion, it has been shown that both caspase-1 and caspase-11 deficient mice are more resistant to endotoxic shock than wild-type controls [64,76].…”

Section: Pyroptosis and The Inflammasomementioning

confidence: 91%

“…Indeed, caspase-11 deficient mice were unable to produce IL-1b and IL-18 in response to LPS stimulation [64]. This requirement, however, seems to be stimulus-specific, since caspase-1 could be activated normally in the absence of caspase-11 following Listeria infection [65].…”

Section: Pyroptosis and The Inflammasomementioning

confidence: 99%

Cell death during sepsis: integration of disintegration in the inflammatory response to overwhelming infection

Silva

Nizet

2009

Apoptosis

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Sepsis is a major health problem and a leading cause of death worldwide. In recent years, a crescendo of attention has been directed to the mechanisms of cell death that develop during this disease, since these are viewed as important contributors to the proinflammatory and antiinflammatory responses associated with poor outcome. Here we discuss mechanisms of cell death evident severe bacterial infection and sepsis including necrosis, apoptosis, pyroptosis, and extracellular trap-associated neutrophil death, with a particular emphasis on lymphocyte apoptosis and its contribution to the immunosuppressed phenotype of late sepsis. Individual bacterial pathogens express virulence factors that modulate cell death pathways and influence the sepsis phenotype. A greater knowledge of cell death pathways in sepsis informs the potential for future therapies designed to ameliorate immune dysfunction in this syndrome.

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Murine Caspase-11, an ICE-Interacting Protease, Is Essential for the Activation of ICE

Cited by 650 publications

References 33 publications

CASP4/caspase-11 promotes autophagosome formation in response to bacterial infection

CASP4/caspase-11 promotes autophagosome formation in response to bacterial infection

Inflammatory caspases and inflammasomes: master switches of inflammation

Cell death during sepsis: integration of disintegration in the inflammatory response to overwhelming infection

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