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  • 1
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    BAFF-R, a newly identified TNF receptor that specifically interacts with BAFF (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-18
    Description: B cell homeostasis has been shown to critically depend on BAFF, the B cell activation factor from the tumor necrosis factor (TNF) family. Although BAFF is already known to bind two receptors, BCMA and TACI, we have identified a third receptor for BAFF that we have termed BAFF-R. BAFF-R binding appears to be highly specific for BAFF, suggesting a unique role for this ligand-receptor interaction. Consistent with this, the BAFF-R locus is disrupted in A/WySnJ mice, which display a B cell phenotype qualitatively similar to that of the BAFF-deficient mice. Thus, BAFF-R appears to be the principal receptor for BAFF-mediated mature B cell survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, J S -- Bixler, S A -- Qian, F -- Vora, K -- Scott, M L -- Cachero, T G -- Hession, C -- Schneider, P -- Sizing, I D -- Mullen, C -- Strauch, K -- Zafari, M -- Benjamin, C D -- Tschopp, J -- Browning, J L -- Ambrose, C -- New York, N.Y. -- Science. 2001 Sep 14;293(5537):2108-11. Epub 2001 Aug 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biogen, 12 Cambridge Center, Cambridge, MA 02142, USA., The Institute of Biochemistry, University of Lausanne, CH-1066, Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509692" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Cell Activating Factor ; B-Cell Activation Factor Receptor ; B-Cell Maturation Antigen ; B-Lymphocytes/immunology/metabolism/*physiology ; Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 22 ; Cloning, Molecular ; Homeostasis ; Humans ; Ligands ; Lymphoid Tissue/metabolism ; Male ; Membrane Proteins/*metabolism ; Mice ; Mice, Inbred A ; Mice, Inbred C57BL ; Molecular Sequence Data ; RNA, Messenger/chemistry/genetics/metabolism ; Receptors, Tumor Necrosis Factor/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection ; Transmembrane Activator and CAML Interactor Protein ; Tumor Necrosis Factor-alpha/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-02-22
    Description: The innate immune system recognizes nucleic acids during infection and tissue damage. Whereas viral RNA is detected by endosomal toll-like receptors (TLR3, TLR7, TLR8) and cytoplasmic RIG-I and MDA5, endosomal TLR9 and cytoplasmic DAI bind DNA, resulting in the activation of nuclear factor-kappaB and interferon regulatory factor transcription factors. However, viruses also trigger pro-inflammatory responses, which remain poorly defined. Here we show that internalized adenoviral DNA induces maturation of pro-interleukin-1beta in macrophages, which is dependent on NALP3 and ASC, components of the innate cytosolic molecular complex termed the inflammasome. Correspondingly, NALP3- and ASC-deficient mice display reduced innate inflammatory responses to adenovirus particles. Inflammasome activation also occurs as a result of transfected cytosolic bacterial, viral and mammalian (host) DNA, but in this case sensing is dependent on ASC but not NALP3. The DNA-sensing pro-inflammatory pathway functions independently of TLRs and interferon regulatory factors. Thus, in addition to viral and bacterial components or danger signals in general, inflammasomes sense potentially dangerous cytoplasmic DNA, strengthening their central role in innate immunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muruve, Daniel A -- Petrilli, Virginie -- Zaiss, Anne K -- White, Lindsay R -- Clark, Sharon A -- Ross, P Joel -- Parks, Robin J -- Tschopp, Jurg -- England -- Nature. 2008 Mar 6;452(7183):103-7. doi: 10.1038/nature06664. Epub 2008 Feb 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of Calgary, Alberta T2N 4N1, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18288107" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics/immunology/physiology ; Animals ; Apoptosis Regulatory Proteins ; Carrier Proteins/genetics/*immunology ; Cell Line ; Cytoskeletal Proteins/deficiency/genetics/*immunology ; Cytosol/*metabolism/microbiology/*virology ; DNA/*immunology ; DNA, Viral/immunology ; Humans ; Immunity, Innate/*immunology ; Inflammation/*immunology/virology ; Interleukin-1beta/immunology/metabolism/secretion ; Macrophages, Peritoneal/immunology/metabolism ; Mice ; Mice, Inbred C57BL ; Protein Processing, Post-Translational
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Syk kinase signalling couples to the Nlrp3 inflammasome for anti-fungal host defence (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-04-03
    Description: Fungal infections represent a serious threat, particularly in immunocompromised patients. Interleukin-1beta (IL-1beta) is a key pro-inflammatory factor in innate antifungal immunity. The mechanism by which the mammalian immune system regulates IL-1beta production after fungal recognition is unclear. Two signals are generally required for IL-1beta production: an NF-kappaB-dependent signal that induces the synthesis of pro-IL-1beta (p35), and a second signal that triggers proteolytic pro-IL-1beta processing to produce bioactive IL-1beta (p17) via Caspase-1-containing multiprotein complexes called inflammasomes. Here we demonstrate that the tyrosine kinase Syk, operating downstream of several immunoreceptor tyrosine-based activation motif (ITAM)-coupled fungal pattern recognition receptors, controls both pro-IL-1beta synthesis and inflammasome activation after cell stimulation with Candida albicans. Whereas Syk signalling for pro-IL-1beta synthesis selectively uses the Card9 pathway, inflammasome activation by the fungus involves reactive oxygen species production and potassium efflux. Genetic deletion or pharmalogical inhibition of Syk selectively abrogated inflammasome activation by C. albicans but not by inflammasome activators such as Salmonella typhimurium or the bacterial toxin nigericin. Nlrp3 (also known as NALP3) was identified as the critical NOD-like receptor family member that transduces the fungal recognition signal to the inflammasome adaptor Asc (Pycard) for Caspase-1 (Casp1) activation and pro-IL-1beta processing. Consistent with an essential role for Nlrp3 inflammasomes in antifungal immunity, we show that Nlrp3-deficient mice are hypersusceptible to Candida albicans infection. Thus, our results demonstrate the molecular basis for IL-1beta production after fungal infection and identify a crucial function for the Nlrp3 inflammasome in mammalian host defence in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gross, Olaf -- Poeck, Hendrik -- Bscheider, Michael -- Dostert, Catherine -- Hannesschlager, Nicole -- Endres, Stefan -- Hartmann, Gunther -- Tardivel, Aubry -- Schweighoffer, Edina -- Tybulewicz, Victor -- Mocsai, Attila -- Tschopp, Jurg -- Ruland, Jurgen -- MC_U117527252/Medical Research Council/United Kingdom -- England -- Nature. 2009 May 21;459(7245):433-6. doi: 10.1038/nature07965. Epub 2009 Apr 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉III. Medizinische Klinik, Klinikum rechts der Isar, Technische Universitat Munchen, Ismaninger Str. 22, 81675 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19339971" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Candida albicans/*immunology/physiology ; Carrier Proteins/*immunology/*metabolism ; Caspase 1/metabolism ; Enzyme Activation ; Humans ; Inflammation/immunology ; Interleukin-1beta/biosynthesis/immunology ; Intracellular Signaling Peptides and Proteins/antagonists & ; inhibitors/deficiency/genetics/*metabolism ; Macrophages/metabolism ; Mice ; Monocytes/metabolism ; Nigericin/pharmacology ; Potassium/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/deficiency/genetics/*metabolism ; Reactive Oxygen Species/metabolism ; *Signal Transduction
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
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    T cells dampen innate immune responses through inhibition of NLRP1 and NLRP3 inflammasomes (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-06-06
    Description: Inflammation is a protective attempt by the host to remove injurious stimuli and initiate the tissue healing process. The inflammatory response must be actively terminated, however, because failure to do so can result in 'bystander' damage to tissues and diseases such as arthritis or type-2 diabetes. Yet the mechanisms controlling excessive inflammatory responses are still poorly understood. Here we show that mouse effector and memory CD4(+) T cells abolish macrophage inflammasome-mediated caspase-1 activation and subsequent interleukin 1beta release in a cognate manner. Inflammasome inhibition is observed for all tested NLRP1 (commonly called NALP1) and NLRP3 (NALP3 or cryopyrin) activators, whereas NLRC4 (IPAF) inflammasome function and release of other inflammatory mediators such as CXCL2, interleukin 6 and tumour necrosis factor are not affected. Suppression of the NLRP3 inflammasome requires cell-to-cell contact and can be mimicked by macrophage stimulation with selected ligands of the tumour necrosis factor family, such as CD40L (also known as CD40LG). In a NLRP3-dependent peritonitis model, effector CD4(+) T cells are responsible for decreasing neutrophil recruitment in an antigen-dependent manner. Our findings reveal an unexpected mechanism of inflammasome inhibition, whereby effector and memory T cells suppress potentially damaging inflammation, yet leave the primary inflammatory response, crucial for the onset of immunity, intact.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guarda, Greta -- Dostert, Catherine -- Staehli, Francesco -- Cabalzar, Katrin -- Castillo, Rosa -- Tardivel, Aubry -- Schneider, Pascal -- Tschopp, Jurg -- England -- Nature. 2009 Jul 9;460(7252):269-73. doi: 10.1038/nature08100. Epub 2009 Jun 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Lausanne, Chemin des Boveresses 155, CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19494813" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*antagonists & inhibitors/metabolism ; Animals ; Antigens/immunology ; Apoptosis Regulatory Proteins/*antagonists & inhibitors/metabolism ; Bone Marrow Cells/cytology ; CD4-Positive T-Lymphocytes/*immunology ; Carrier Proteins/*antagonists & inhibitors/metabolism ; Caspase 1/metabolism ; Cells, Cultured ; Immunity, Innate/*immunology ; Immunologic Memory ; Inflammation/immunology/*metabolism/pathology ; Interleukin-1beta/immunology ; Ligands ; Macrophages/immunology ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Neutrophils/immunology ; Peritoneal Cavity/cytology ; Tumor Necrosis Factors/immunology/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-04-12
    Description: The inhalation of airborne pollutants, such as asbestos or silica, is linked to inflammation of the lung, fibrosis, and lung cancer. How the presence of pathogenic dust is recognized and how chronic inflammatory diseases are triggered are poorly understood. Here, we show that asbestos and silica are sensed by the Nalp3 inflammasome, whose subsequent activation leads to interleukin-1beta secretion. Inflammasome activation is triggered by reactive oxygen species, which are generated by a NADPH oxidase upon particle phagocytosis. (NADPH is the reduced form of nicotinamide adenine dinucleotide phosphate.) In a model of asbestos inhalation, Nalp3-/- mice showed diminished recruitment of inflammatory cells to the lungs, paralleled by lower cytokine production. Our findings implicate the Nalp3 inflammasome in particulate matter-related pulmonary diseases and support its role as a major proinflammatory "danger" receptor.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2396588/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2396588/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dostert, Catherine -- Petrilli, Virginie -- Van Bruggen, Robin -- Steele, Chad -- Mossman, Brooke T -- Tschopp, Jurg -- P01 CA114047/CA/NCI NIH HHS/ -- P01 CA114047-01A10002/CA/NCI NIH HHS/ -- P01HL67004/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2008 May 2;320(5876):674-7. doi: 10.1126/science.1156995. Epub 2008 Apr 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Lausanne, Chemin des Boveresses 155, 1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18403674" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Asbestos/*immunology ; Carrier Proteins/*physiology ; Humans ; Immunity ; Inflammation/*immunology ; Inflammation Mediators/*physiology ; Interleukin-1beta/secretion ; Macrophages/immunology/secretion ; Mice ; Silicon Dioxide/*immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Inhibition of toxic epidermal necrolysis by blockade of CD95 with human intravenous immunoglobulin (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-17
    Description: Toxic epidermal necrolysis (TEN, Lyell's syndrome) is a severe adverse drug reaction in which keratinocytes die and large sections of epidermis separate from the dermis. Keratinocytes normally express the death receptor Fas (CD95); those from TEN patients were found to express lytically active Fas ligand (FasL). Antibodies present in pooled human intravenous immunoglobulins (IVIG) blocked Fas-mediated keratinocyte death in vitro. In a pilot study, 10 consecutive individuals with clinically and histologically confirmed TEN were treated with IVIG; disease progression was rapidly reversed and the outcome was favorable in all cases. Thus, Fas-FasL interactions are directly involved in the epidermal necrolysis of TEN, and IVIG may be an effective treatment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Viard, I -- Wehrli, P -- Bullani, R -- Schneider, P -- Holler, N -- Salomon, D -- Hunziker, T -- Saurat, J H -- Tschopp, J -- French, L E -- New York, N.Y. -- Science. 1998 Oct 16;282(5388):490-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, Geneva University Medical School, CH-1211 Geneva 4, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9774279" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Aged ; Aged, 80 and over ; Antibodies, Blocking/immunology/therapeutic use ; Antigens, CD95/immunology/*physiology ; *Apoptosis ; Child ; Dermis/pathology ; Disease Progression ; Epidermis/pathology ; Fas Ligand Protein ; Female ; Humans ; Immunoglobulins, Intravenous/*therapeutic use ; Jurkat Cells ; Keratinocytes/metabolism/*pathology ; Male ; Membrane Glycoproteins/metabolism ; Middle Aged ; Pilot Projects ; Stevens-Johnson Syndrome/pathology/*therapy
    Print ISSN: 0036-8075
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  • 7
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    The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-10
    Description: Apoptosis is triggered by activation of initiator caspases upon complex-mediated clustering of the inactive zymogen, as occurs in the caspase-9-activating apoptosome complex. Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular composition of which remains elusive. We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD. Increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli. Because PIDD functions in p53-mediated apoptosis, the complex assembled by PIDD and caspase-2 is likely to regulate apoptosis induced by genotoxins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tinel, Antoine -- Tschopp, Jurg -- New York, N.Y. -- Science. 2004 May 7;304(5672):843-6. Epub 2004 Apr 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Lausanne, Chemin des Boveresses 155, CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15073321" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; *Apoptosis ; CRADD Signaling Adaptor Protein ; Carrier Proteins/chemistry/*metabolism ; Caspase 2 ; Caspases/*metabolism ; Cell Line ; Cell Line, Tumor ; Cloning, Molecular ; *DNA Damage ; Death Domain Receptor Signaling Adaptor Proteins ; Doxorubicin/pharmacology ; Enzyme Activation ; Etoposide/pharmacology ; Humans ; Protein Structure, Tertiary ; Proteins/chemistry/metabolism ; RNA, Small Interfering ; Signal Transduction ; Transfection ; Tumor Suppressor Protein p53/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    A role for mitochondria in NLRP3 inflammasome activation (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-12-03
    Description: An inflammatory response initiated by the NLRP3 inflammasome is triggered by a variety of situations of host 'danger', including infection and metabolic dysregulation. Previous studies suggested that NLRP3 inflammasome activity is negatively regulated by autophagy and positively regulated by reactive oxygen species (ROS) derived from an uncharacterized organelle. Here we show that mitophagy/autophagy blockade leads to the accumulation of damaged, ROS-generating mitochondria, and this in turn activates the NLRP3 inflammasome. Resting NLRP3 localizes to endoplasmic reticulum structures, whereas on inflammasome activation both NLRP3 and its adaptor ASC redistribute to the perinuclear space where they co-localize with endoplasmic reticulum and mitochondria organelle clusters. Notably, both ROS generation and inflammasome activation are suppressed when mitochondrial activity is dysregulated by inhibition of the voltage-dependent anion channel. This indicates that NLRP3 inflammasome senses mitochondrial dysfunction and may explain the frequent association of mitochondrial damage with inflammatory diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, Rongbin -- Yazdi, Amir S -- Menu, Philippe -- Tschopp, Jurg -- England -- Nature. 2011 Jan 13;469(7329):221-5. doi: 10.1038/nature09663. Epub 2010 Dec 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Center of Immunity and Infection, University of Lausanne, Chemin des Boveresses 155, CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21124315" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis Regulatory Proteins ; Autophagy/drug effects ; Carrier Proteins/genetics/*metabolism ; Cell Line ; Cytoskeletal Proteins/genetics/metabolism ; Endoplasmic Reticulum/metabolism ; Humans ; Immunity, Innate ; Inflammasomes/drug effects/*metabolism ; Inflammation/metabolism/pathology ; Interleukin-1beta/metabolism/secretion ; Macrophages/cytology/metabolism/pathology/secretion ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Mice, Transgenic ; Mitochondria/drug effects/*metabolism/pathology ; Reactive Oxygen Species/metabolism ; Thioredoxins/genetics/metabolism ; Voltage-Dependent Anion Channels/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
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    Melanoma cell expression of Fas(Apo-1/CD95) ligand: implications for tumor immune escape (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: Malignant melanoma accounts for most of the increasing mortality from skin cancer. Melanoma cells were found to express Fas (also called Apo-1 or CD95) ligand (FasL). In metastatic lesions, Fas-expressing T cell infiltrates were proximal to FasL+ tumor cells. In vitro, apoptosis of Fas-sensitive target cells occurred upon incubation with melanoma tumor cells; and in vivo, injection of FasL+ mouse melanoma cells in mice led to rapid tumor formation. In contrast, tumorigenesis was delayed in Fas-deficient lpr mutant mice in which immune effector cells cannot be killed by FasL. Thus, FasL may contribute to the immune privilege of tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahne, M -- Rimoldi, D -- Schroter, M -- Romero, P -- Schreier, M -- French, L E -- Schneider, P -- Bornand, T -- Fontana, A -- Lienard, D -- Cerottini, J -- Tschopp, J -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Biochemistry, University of Lausanne, CH-1066 Epalinges, Switzerland. jurg.tschopp@ib.unil.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910274" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD95/biosynthesis/*physiology ; *Apoptosis ; Fas Ligand Protein ; Humans ; Ligands ; Lymphocytes, Tumor-Infiltrating/cytology/immunology ; Melanoma/*immunology/metabolism/pathology/secondary ; Membrane Glycoproteins/analysis/biosynthesis/*physiology ; Mice ; Mice, Inbred C57BL ; T-Lymphocytes, Cytotoxic/*cytology/immunology ; Tumor Cells, Cultured ; *Tumor Escape
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    The NLRP3 inflammasome: a sensor for metabolic danger? (2010)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2010-01-16
    Description: Interleukin-1beta (IL-1beta), reactive oxygen species (ROS), and thioredoxin-interacting protein (TXNIP) are all implicated in the pathogenesis of type 2 diabetes mellitus (T2DM). Here we review mechanisms directing IL-1beta production and its pathogenic role in islet dysfunction during chronic hyperglycemia. In doing so, we integrate previously disparate disease-driving mechanisms for IL-1beta, ROS, and TXNIP in T2DM into one unifying model in which the NLRP3 inflammasome plays a central role. The NLRP3 inflammasome also drives IL-1beta maturation and secretion in another disease of metabolic dysregulation, gout. Thus, we propose that the NLRP3 inflammasome contributes to the pathogenesis of T2DM and gout by functioning as a sensor for metabolic stress.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schroder, Kate -- Zhou, Rongbin -- Tschopp, Jurg -- New York, N.Y. -- Science. 2010 Jan 15;327(5963):296-300. doi: 10.1126/science.1184003.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Lausanne, CH-1066 Epalinges, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20075245" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/*metabolism ; Diabetes Mellitus, Type 2/immunology/*metabolism/physiopathology ; Gout/immunology/metabolism ; Humans ; *Inflammation ; Insulin-Secreting Cells/physiology ; Interleukin-1beta/metabolism/secretion ; Multiprotein Complexes/*metabolism ; Reactive Oxygen Species/metabolism ; *Stress, Physiological
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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