TNFR1-dependent cell death drives inflammation in Sharpin-deficient mice

  • James A Rickard
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Holly Anderton
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Nima Etemadi
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Ueli Nachbur
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Maurice Darding
    Centre for Cell Death, Cancer, and Inflammation, University College London, London, United Kingdom
  • Nieves Peltzer
    Centre for Cell Death, Cancer, and Inflammation, University College London, London, United Kingdom
  • Najoua Lalaoui
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Kate E Lawlor
    Department of Medical Biology, University of Melbourne, Parkville, Australia
  • Hannah Vanyai
    Department of Medical Biology, University of Melbourne, Parkville, Australia
  • Cathrine Hall
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Aleks Bankovacki
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Lahiru Gangoda
    Department of Biochemistry, La Trobe University, Bundoora, Australia
  • Wendy Wei-Lynn Wong
    Department of Immunology, Institute of Experimental Immunology, University of Zurich, Zurich, Switzerland
  • Jason Corbin
    Department of Medical Biology, University of Melbourne, Parkville, Australia
  • Chunzi Huang
    Department of Microbiology and Immunology, Emory Vaccine Center, Emory University School of Medicine, Atlanta, United States
  • Edward S Mocarski
    Department of Microbiology and Immunology, Emory Vaccine Center, Emory University School of Medicine, Atlanta, United States
  • James M Murphy
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • Warren S Alexander
    Department of Medical Biology, University of Melbourne, Parkville, Australia
  • Anne K Voss
    Department of Medical Biology, University of Melbourne, Parkville, Australia
  • David L Vaux
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
  • William J Kaiser
    Department of Microbiology and Immunology, Emory Vaccine Center, Emory University School of Medicine, Atlanta, United States
  • Henning Walczak
    Centre for Cell Death, Cancer, and Inflammation, University College London, London, United Kingdom
  • John Silke
    Cell Signalling and Cell Death Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia

書誌事項

公開日
2014-12-02
権利情報
  • http://creativecommons.org/licenses/by/4.0/
  • http://creativecommons.org/licenses/by/4.0/
  • http://creativecommons.org/licenses/by/4.0/
DOI
  • 10.7554/elife.03464
公開者
eLife Sciences Publications, Ltd

説明

<jats:p>SHARPIN regulates immune signaling and contributes to full transcriptional activity and prevention of cell death in response to TNF in vitro. The inactivating mouse Sharpin cpdm mutation causes TNF-dependent multi-organ inflammation, characterized by dermatitis, liver inflammation, splenomegaly, and loss of Peyer's patches. TNF-dependent cell death has been proposed to cause the inflammatory phenotype and consistent with this we show Tnfr1, but not Tnfr2, deficiency suppresses the phenotype (and it does so more efficiently than Il1r1 loss). TNFR1-induced apoptosis can proceed through caspase-8 and BID, but reduction in or loss of these players generally did not suppress inflammation, although Casp8 heterozygosity significantly delayed dermatitis. Ripk3 or Mlkl deficiency partially ameliorated the multi-organ phenotype, and combined Ripk3 deletion and Casp8 heterozygosity almost completely suppressed it, even restoring Peyer's patches. Unexpectedly, Sharpin, Ripk3 and Casp8 triple deficiency caused perinatal lethality. These results provide unexpected insights into the developmental importance of SHARPIN.</jats:p>

収録刊行物

  • eLife

    eLife 3 e03464-, 2014-12-02

    eLife Sciences Publications, Ltd

被引用文献 (17)*注記

もっと見る

問題の指摘

ページトップへ