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Positive Regulation of Interleukin-1ß Bioactivity by Physiological ROS-Mediated Cysteine S-Glutathionylation.
Zhang, Xue; Liu, Peng; Zhang, Christie; Chiewchengchol, Direkrit; Zhao, Fan; Yu, Hongbo; Li, Jingyu; Kambara, Hiroto; Luo, Kate Y; Venkataraman, Arvind; Zhou, Ziling; Zhou, Weidong; Zhu, Haiyan; Zhao, Li; Sakai, Jiro; Chen, Yuanyuan; Ho, Ye-Shih; Bajrami, Besnik; Xu, Bing; Silberstein, Leslie E; Cheng, Tao; Xu, Yuanfu; Ke, Yuehai; Luo, Hongbo R.
Afiliação
  • Zhang X; Department of Pathology and Pathophysiology, Program in Molecular Cell Biology, Zhejiang University School of Medicine, Hangzhou 310058, China; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer C
  • Liu P; The State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Diseases Hospital, Center for Stem Cell Medicine, Chinese Academy of Medical Sciences and Peking Union Medical College, 288 Nanjing Road, Tianjin 300020, China.
  • Zhang C; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Chiewchengchol D; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Zhao F; The State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Diseases Hospital, Center for Stem Cell Medicine, Chinese Academy of Medical Sciences and Peking Union Medical College, 288 Nanjing Road, Tianjin 300020, China.
  • Yu H; Hematopathology, Flow Cytometry, Hematology, and Blood Bank Labs, VA Boston Healthcare System, West Roxbury, MA 02132, USA; Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 01605, USA.
  • Li J; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Kambara H; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Luo KY; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Venkataraman A; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Zhou Z; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Zhou W; Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, VA 20110, USA.
  • Zhu H; The State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Diseases Hospital, Center for Stem Cell Medicine, Chinese Academy of Medical Sciences and Peking Union Medical College, 288 Nanjing Road, Tianjin 300020, China.
  • Zhao L; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Sakai J; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Chen Y; Department of Pathology and Pathophysiology, Program in Molecular Cell Biology, Zhejiang University School of Medicine, Hangzhou 310058, China; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer C
  • Ho YS; Institute of Environmental Health Sciences and Department of Biochemistry and Molecular Biology, Wayne State University, Detroit, MI 48201, USA.
  • Bajrami B; Mass Spectrometry Unit, Waters Corporation, Milford, MA 01757, USA.
  • Xu B; Department of Chemistry, Brandeis University, 415 South Street MS015, Waltham, MA 02454, USA.
  • Silberstein LE; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Cheng T; The State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Diseases Hospital, Center for Stem Cell Medicine, Chinese Academy of Medical Sciences and Peking Union Medical College, 288 Nanjing Road, Tianjin 300020, China.
  • Xu Y; The State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Diseases Hospital, Center for Stem Cell Medicine, Chinese Academy of Medical Sciences and Peking Union Medical College, 288 Nanjing Road, Tianjin 300020, China.
  • Ke Y; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA.
  • Luo HR; Department of Pathology, Harvard Medical School, Boston, MA 02115, USA; Department of Lab Medicine, Children's Hospital Boston, Dana-Farber/Harvard Cancer Center, Boston, MA 02115, USA. Electronic address: hongbo.luo@childrens.harvard.edu.
Cell Rep ; 20(1): 224-235, 2017 07 05.
Article em En | MEDLINE | ID: mdl-28683316
Reactive oxygen species (ROS)-induced cysteine S-glutathionylation is an important posttranslational modification (PTM) that controls a wide range of intracellular protein activities. However, whether physiological ROS can modulate the function of extracellular components via S-glutathionylation is unknown. Using a screening approach, we identified ROS-mediated cysteine S-glutathionylation on several extracellular cytokines. Glutathionylation of the highly conserved Cys-188 in IL-1ß positively regulates its bioactivity by preventing its ROS-induced irreversible oxidation, including sulfinic acid and sulfonic acid formation. We show this mechanism protects IL-1ß from deactivation by ROS in an in vivo system of irradiation-induced bone marrow (BM) injury. Glutaredoxin 1 (Grx1), an enzyme that catalyzes deglutathionylation, was present and active in the extracellular space in serum and the BM, physiologically regulating IL-1ß glutathionylation and bioactivity. Collectively, we identify cysteine S-glutathionylation as a cytokine regulatory mechanism that could be a therapeutic target in the treatment of various infectious and inflammatory diseases.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Processamento de Proteína Pós-Traducional / Espécies Reativas de Oxigênio / Interleucina-1beta / Glutationa Limite: Animals Idioma: En Revista: Cell Rep Ano de publicação: 2017 Tipo de documento: Article País de publicação: Estados Unidos
Texto completo
Adicionar na Minha BVS
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Processamento de Proteína Pós-Traducional / Espécies Reativas de Oxigênio / Interleucina-1beta / Glutationa Limite: Animals Idioma: En Revista: Cell Rep Ano de publicação: 2017 Tipo de documento: Article País de publicação: Estados Unidos