New Mutations of CIAS1 That Are Responsible for Muckle-Wells Syndrome and Familial Cold Urticaria: A Novel Mutation Underlies Both Syndromes

Dodé, Catherine; Dû, Nathalie Le; Cuisset, Laurence; Letourneur, Frank; Berthelot, Jean‐Marie; Vaudour, G; Meyrier, Alain; Watts, Richard A.; Scott, G.I. David; Nicholls, Anne; Granel, B.; Françès, Camille; Garcier, F; Edery, Patrick; Boulinguez, S.; Domergues, Jean-Paul; Delpech, Marc; Grateau, Gilles

doi:10.1086/340786

Cited by 282 publications

(202 citation statements)

References 22 publications

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“…MWS is associated with heterozygous mutations in CIAS1, and the R260W amino acid mutation recognized in our patient has been previously reported (10). CIAS1 mutations were identified as the cause of FCAS, MWS, and NOMID/CINCA syndrome.…”

Section: Discussionsupporting

confidence: 69%

Anakinra improves sensory deafness in a Japanese patient with Muckle‐Wells syndrome, possibly by inhibiting the cryopyrin inflammasome

Yamazaki¹,

Masumoto²,

Agematsu³

et al. 2008

Arthritis & Rheumatism

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Muckle-Wells syndrome (MWS) is a dominantly inherited autoinflammatory syndrome. Patients withMWS have a mutation in CIAS1, the gene encoding cryopyrin, a component of the inflammasome that regulates the processing of interleukin-1␤ (IL-1␤). In this report we describe an 8-year-old Japanese girl with MWS who had symptoms of periodic fever, urticarial rash, conjunctivitis, arthropathy, and sensory deafness. Laboratory analysis of the patient's serum showed abnormally high concentrations of C-reactive protein, serum amyloid A, and IL-1␤, and she had a heterozygous mutation in the CIAS1 gene, with C-to-T transversion at nucleotide position 778, encoding an arginineto-tryptophan mutation at position 260 (R260W). Mononuclear cells (MNCs) isolated from the patient secreted large amounts of IL-1␤, without stimulation, and were highly sensitive to muramyldipeptide and lipopolysaccharide. After treatment with anakinra, laboratory results normalized, and clinical symptoms, including sensory deafness, disappeared, while MNCs appeared to remain activated. Thus, our case suggests that anakinra possibly affects the cryopyrin inflammasome and markedly improves the clinical and laboratory manifestations of MWS.

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Section: Discussionsupporting

confidence: 69%

Anakinra improves sensory deafness in a Japanese patient with Muckle‐Wells syndrome, possibly by inhibiting the cryopyrin inflammasome

Yamazaki¹,

Masumoto²,

Agematsu³

et al. 2008

Arthritis & Rheumatism

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“…66,86,87 All three disorders are closely related autoinflammatory syndromes characterized by periodic fever, skin rashes, amyloidosis and in the case of CINCA, the eventual development of neurological complications. Mutations in NALP3 confer a gain of function to the protein, resulting in constitutively active NALP3 in Muckle Wells patients.…”

Section: Nalp3 Inflammasome and Autoinflammatory Disordersmentioning

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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“…These patients have chronic systemic inflammation involving the skin, joints, and central nervous system, and also have cartilage overgrowth, hearing loss, and eye disease (Prieur et al, 1987). There is some correlation of specific CIAS1 nucleotide substitutions with phenotype; however, the same mutation has been associated with different phenotypes in different patients suggesting additional genetic or environmental influences (Dode et al, 2002;Neven et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Structural, expression, and evolutionary analysis of mouse CIAS1

Anderson

Mueller

Rosengren

et al. 2004

Gene

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Mutations in the human CIAS1 (hCIAS1) gene have been identified in a continuum of inflammatory disorders including familial cold autoinflammatory syndrome (FCAS), MuckleWells syndrome (MWS), and neonatal onset multisystem inflammatory disease (NOMID). CIAS1 codes for the protein Cryopyrin, which appears to play a role in innate immune function by regulating the production of proinflammatory cytokines. Human and mouse Cryopyrin are highly conserved and consist of three functional domains including a pyrin domain, an NACHT domain, ☆ Supplementary data associated with this article can be found, in the online version, at doi: 10.1016/j.gene.2004.05.002.☆☆ The nucleotide sequence data reported in this paper have been submitted to GenBank and have been assigned the accession numbers for the three mouse strains (strain C57BL/6) CIAS1.mRNAThe primate sequence accession numbers are GgCIAS1.Exon1 AY337307, TgCIAS1.Exon1 AY337308, MsCIAS1.Exon1 AY337309, AbCIAS1.Exon1 AY337310, CjCIAS1.Exon1 AY337311, CmCIAS1.Exon1 AY337312, GgCIAS1.NBS AY338196, TgCIAS1.NBS AY338197, MsCIAS1.NBS AY338198, CcCIAS1.NBS AY338199, CgCIAS1.NBS AY338200, AbCIAS1.NBS AY338201, AaCIAS1.NBS AY338202, SsCIAS1.NBS AY338203, CaCIAS1.NBS AY338204, S.CIAS1.NBS AY338205, CjCIAS1.NBS AY338206, Cp.CIAS1.NBS AY338207, TbCIAS1.NBS AY338208, CmCIAS1.NBS AY338209, LcCIAS1.NBS AY338210, and VvCIAS1.NBS AY338211. The mammalian sequence accession numbers are LaCIAS1.NBS AY495378, EeCIAS1.NBS AY495379, and DnCIAS1.NBS AY495380. and a leucine-rich repeat (LRR) domain that are characteristics of the NALP family of proteins. The pyrin and NACHT domains of Cryopyrin and other NALP proteins are highly conserved among primate and nonprimate mammals, suggesting purifying selection throughout mammalian evolution. Cryopyrin expression is also very similar in human and mouse with mouse CIAS1 mRNA expression found primarily in peripheral blood leukocytes consistent with the postulated inflammatory function. We also detected significant expression in mouse eye and skin tissue, which is consistent with symptoms observed in human Cryopyrin-associated diseases. HHS Public Access

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New Mutations of CIAS1 That Are Responsible for Muckle-Wells Syndrome and Familial Cold Urticaria: A Novel Mutation Underlies Both Syndromes

Cited by 282 publications

References 22 publications

Anakinra improves sensory deafness in a Japanese patient with Muckle‐Wells syndrome, possibly by inhibiting the cryopyrin inflammasome

Anakinra improves sensory deafness in a Japanese patient with Muckle‐Wells syndrome, possibly by inhibiting the cryopyrin inflammasome

Inflammatory caspases and inflammasomes: master switches of inflammation

Structural, expression, and evolutionary analysis of mouse CIAS1

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