Martinon, F., Hofmann, K. & Tschopp, J. The Pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation. Curr. Biol. 10, R118-R120

Current Biology (Impact Factor: 9.57). 03/2001; 11(4):R118-20. DOI: 10.1016/S0960-9822(01)00056-2
Source: PubMed
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    • "The locus for familial vitiligo on chromosome 17 was recently demonstrated to harbor the gene coding for NALP1.[4] NALP1(NACHT-LRR-PYD- containing protein- 1), together with the related protein NALP2, has been identified by Martinon et al.[5] in a databank search for proteins containing a pyrin domain. The protein contains a NACHT domain, an LRR domain (leucine-rich repeat), and a pyrin domain. "
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    ABSTRACT: Vitiligo is an acquired autoimmune disease of unknown etiology showing depigmentation of the skin due to the absence of melanocytes. Familial vitiligo suggests a genetic origin to this disease. Chromosome 17 was recently demonstrated to harbor the gene coding for NALP1. A total of 18 patients of vitiligo were selected on the basis of clinical history. Group 1 (N=8) showing segmental or localized vitiligo with one or two macules on the body. Group 2 (N=10) with generalized or whole body vitiligo. A control group of 10 healthy individuals were selected from our laboratory persons with no history or any infections or skin disease. NALP1 gene expression was studied using RT-PCR assay and the bands quantitated as intensity using volume as measurement and comparison of results was done using SPSS 16 version for statistical analysis. NALP1 gene expression was observed in vitiligo patients with different intensities. Greater reduction in the intensity was seen in Group I, which was inversely proportional to the volume of the band. The intensity of the NALP1 and the GAPDH gene expression was more in Group 2 patients than that shown by Group 1. This study shows expression of NALP1 gene in patients as well as normals. NALP1 is widely expressed at low levels but is expressed at high levels in immune cells, particularly T cells and Langerhans cells, in which different patterns are seen that are consistent with the particular involvement of NALP1 in skin autoimmunity.
    Indian Journal of Dermatology 05/2011; 56(3):266-71. DOI:10.4103/0019-5154.82478
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    • "The adaptor ASC (also known as PYCARD) has an N-terminal PYD that facilitates interactions with the PYD domain of NLRs, and a C-terminal CARD domain that recruits caspase-1 through CARD-CARD interactions (Martinon et al., 2001). Interestingly, besides its role as an adaptor, ASC is required to induce autoproteolysis of pro-caspase-1 in the inflammasome complex, a prerequirement for efficient cytokine processing (Broz et al., 2010b). "
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    ABSTRACT: Francisella tularensis is an intracellular pathogen that can cause severe disease in a wide range of mammalian hosts. Primarily residing in host macrophages, F. tularensis escapes phagosomal degradation, and replicates in the macrophage cytosol. The macrophage uses a series of pattern recognition receptors to detect conserved microbial molecules from invading pathogens, and initiates an appropriate host response. In the cytosol, F. tularensis is recognized by the inflammasome, a multiprotein complex responsible for the activation of the cysteine protease caspase-1. Caspase-1 activation leads to processing and release of proinflammatory cytokines and host cell death. Here we review recent work on the molecular mechanisms of inflammasome activation by F. tularensis, and its consequences both in vitro and in vivo. Finally, we discuss the coordination between the inflammasome and other cytosolic host responses, and the evidence for F. tularensis virulence factors that suppress inflammasome activation.
    Frontiers in Microbiology 02/2011; 2:16. DOI:10.3389/fmicb.2011.00016 · 3.99 Impact Factor
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    • "MEFV encodes a 781 amino acids' protein named pyrin or marenostrin (P/M) that is involved in the inflammatory pathways of the innate immune system [6]. Sequence alignment of the protein revealed 6 domains: a pyrin domain (or PyD), a bZIP basic domain, a B-box zinc finger domain, a coiled coil domain, 2 nuclear localization signals domains and a Ret Finger protein (RFP or B30.2) domain, also known as SPRY domain [7,8]. "
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    ABSTRACT: Familial Mediterranean fever is a recessive autoinflammatory disease frequently encountered in Armenians, Jews, Arabs and Turks. The MEFV gene is responsible for the disease. It encodes a protein called pyrin/marenostrin involved in the innate immune system. A large number of clinically diagnosed FMF patients carry only one MEFV mutation. This study aims at studying the MEFV gene splicing pattern in heterozygous FMF patients and healthy individuals, in an attempt to understand the mechanism underlying the disease in these patients. RNA was extracted from peripheral blood leucocytes of 41 FMF patients and 34 healthy individuals. RT-PCR was then performed, and the amplified products were migrated on a polyacrylamide electrophoresis gel, characterized by gel extraction of the corresponding bands followed by sequencing. Five novel splicing events were observed in both patients and controls deleting either exons 3, 4 (del34), or exons 2, 3, 4 (del234), or exons 2, 3, 4, 5 (del2345) or exon7 (del7) or exons 7 and 8 (del78). The observation of such qualitative variability in the expression of the MEFV gene suggests a complex transcriptional regulation. However, the expression of these novel transcripts in both patients and controls is not in favour of a severe pathogenic effect.
    BMC Medical Genetics 06/2010; 11(1):87. DOI:10.1186/1471-2350-11-87 · 2.08 Impact Factor
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