Glutaredoxin 1 up-regulates deglutathionylation of α4 integrin and thereby restricts neutrophil mobilization from bone marrow

Journal of Biological Chemistry - Tập 294 - Trang 2616-5242 - 2019
Yuanyuan You1, Junli Chen1, Feimei Zhu1, Qian Xu1, Lu Han2, Xiang Gao2, Xiaoyu Zhang3, Hongbo R. Luo4,5,6, Junming Miao1, Xiaodong Sun7, Hongyu Ren1, Yu Du1, Lijuan Guo1, Xiaoying Wang1, Yi Wang1, Shanze Chen1, Ning Huang1, Jingyu Li1
1Department of Pathophysiology, Sichuan University, Chengdu 610041, China
2State Key Laboratory of Biotherapy and Cancer Center/Collaborative Innovation Center of Biotherapy, Sichuan University, Chengdu 610041, China
3State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Diseases Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Tianjin 300020, China
4Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115
5Department of Lab Medicine, Children's Hospital Boston, Boston, Massachusetts 02115
6Dana-Farber/Harvard Cancer Center, Boston, Massachusetts 02115
7Department of Pharmacology, West China School of Basic Medical Sciences and Forensic Medicine, Sichuan University, Chengdu, 610041, China

Tài liệu tham khảo

Thomas, 1995, Analysis of cells and tissues for S-thiolation of specific proteins, Methods Enzymol, 251, 423, 10.1016/0076-6879(95)51145-8 Pastore, 2012, S-glutathionylation signaling in cell biology: progress and prospects, Eur. J. Pharm. Sci, 46, 279, 10.1016/j.ejps.2012.03.010 Giganti, 2018, Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity, Nat. Commun, 9, 185, 10.1038/s41467-017-02528-7 Chen, 2010, S-glutathionylation uncouples eNOS and regulates its cellular and vascular function, Nature, 468, 1115, 10.1038/nature09599 Stojkov, 2017, ROS and glutathionylation balance cytoskeletal dynamics in neutrophil extracellular trap formation, J. Cell Biol, 216, 4073, 10.1083/jcb.201611168 Shelton, 2008, Regulation by reversible S-glutathionylation: molecular targets implicated in inflammatory diseases, Mol. Cells, 25, 332 Tafani, 2016, The interplay of reactive oxygen species, hypoxia, inflammation, and sirtuins in cancer initiation and progression, Oxid. Med. Cell Longev, 2016, 10.1155/2016/3907147 Dalle-Donne, 2009, Protein S-glutathionylation: a regulatory device from bacteria to humans, Trends Biochem. Sci, 34, 85, 10.1016/j.tibs.2008.11.002 Holmgren, 1976, Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione, Proc. Natl. Acad. Sci. U.S.A, 73, 2275, 10.1073/pnas.73.7.2275 Kuipers, 2012, Altered cigarette smoke-induced lung inflammation due to ablation of Grx1, PLoS ONE, 7, 10.1371/journal.pone.0038984 Lillig, 2008, Glutaredoxin systems, Biochim. Biophys. Acta, 1780, 1304, 10.1016/j.bbagen.2008.06.003 Fernandes, 2004, Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system, Antioxid. Redox Signal, 6, 63, 10.1089/152308604771978354 Sakai, 2012, Reactive oxygen species-induced actin glutathionylation controls actin dynamics in neutrophils, Immunity, 37, 1037, 10.1016/j.immuni.2012.08.017 Zhang, 2017, Positive regulation of interleukin-1β bioactivity by physiological ROS-mediated cysteine S-glutathionylation, Cell Rep, 20, 224, 10.1016/j.celrep.2017.05.070 Liu, 2008, Ligand binding of leukocyte integrin very late antigen-4 involves exposure of sulfhydryl groups and is subject to redox modulation, Eur. J. Immunol, 38, 410, 10.1002/eji.200737556 Zhao, 2012, Bone marrow and the control of immunity, Cell Mol. Immunol, 9, 11, 10.1038/cmi.2011.47 Burdon, 2005, The CXC chemokine MIP-2 stimulates neutrophil mobilization from the rat bone marrow in a CD49d-dependent manner, Blood, 105, 2543, 10.1182/blood-2004-08-3193 Sadik, 2011, Neutrophils cascading their way to inflammation, Trends Immunol, 32, 452, 10.1016/j.it.2011.06.008 Petty, 2009, Crosstalk between CXCR4/stromal derived factor-1 and VLA-4/VCAM-1 pathways regulates neutrophil retention in the bone marrow, J. Immunol, 182, 604, 10.4049/jimmunol.182.1.604 Hyun, 2017, Deep insight into neutrophil trafficking in various organs, J. Leukoc. Biol, 102, 617, 10.1189/jlb.1RU1216-521R Rettig, 2012, Mobilization of hematopoietic stem and progenitor cells using inhibitors of CXCR4 and VLA-4, Leukemia, 26, 34, 10.1038/leu.2011.197 Peltoniemi, 2006, Modulation of glutaredoxin in the lung and sputum of cigarette smokers and chronic obstructive pulmonary disease, Respir. Res, 7, 133, 10.1186/1465-9921-7-133 Nakamura, 1998, Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery, Free Radic. Biol. Med, 24, 1176, 10.1016/S0891-5849(97)00429-2 Chrestensen, 2000, Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis, J. Biol. Chem, 275, 26556, 10.1074/jbc.M004097200 Zhu, 2017, Reactive oxygen species-producing myeloid cells act as a bone marrow niche for sterile inflammation-induced reactive granulopoiesis, J. Immunol, 198, 2854, 10.4049/jimmunol.1602006 Bajrami, 2016, G-CSF maintains controlled neutrophil mobilization during acute inflammation by negatively regulating CXCR2 signaling, J. Exp. Med, 213, 1999, 10.1084/jem.20160393 Eash, 2010, CXCR2 and CXCR4 antagonistically regulate neutrophil trafficking from murine bone marrow, J. Clin. Invest, 120, 2423, 10.1172/JCI41649 Petit, 2002, G-CSF induces stem cell mobilization by decreasing bone marrow SDF-1 and up-regulating CXCR4, Nat. Immunol, 3, 687, 10.1038/ni813 Shimizu, 1999, Integrins in the immune system, Adv. Immunol, 72, 325, 10.1016/S0065-2776(08)60024-3 Yuan, 2013, The role of ROS in ionizing radiation-induced VLA-4 mediated adhesion of RAW264.7 cells to VCAM-1 under flow conditions, Radiat. Res, 179, 62, 10.1667/RR3119.1 Valcárcel, 2014, IL-18 regulates melanoma VLA-4 integrin activation through a hierarchized sequence of inflammatory factors, J. Invest. Dermatol, 134, 470, 10.1038/jid.2013.342 Popov, 2014, Protein S-glutathionylation: from current basics to targeted modifications, Arch. Physiol. Biochem, 120, 123, 10.3109/13813455.2014.944544 Sevilla, 2015, The thioredoxin/peroxiredoxin/sulfiredoxin system: current overview on its redox function in plants and regulation by reactive oxygen and nitrogen species, J. Exp. Bot, 66, 2945, 10.1093/jxb/erv146 Du, 2014, Plasma glutaredoxin activity in healthy subjects and patients with abnormal glucose levels or overt type 2 diabetes, Acta Diabetol, 51, 225, 10.1007/s00592-013-0498-2 Takada, 1989, The primary structure of the α4 subunit of VLA-4: homology to other integrins and a possible cell-cell adhesion function, EMBO J, 8, 1361, 10.1002/j.1460-2075.1989.tb03516.x Harp, 2005, Adhesion molecule and homing receptor expression on blood and milk polymorphonuclear leukocytes during the periparturient period of dairy cattle, Vet. Immunol. Immunopathol, 104, 99, 10.1016/j.vetimm.2004.10.007 Pujades, 1996, Integrin α4 cysteines 278 and 717 modulate VLA-4 ligand binding and also contribute to α 4/180 formation, Biochem. J, 313, 899, 10.1042/bj3130899 Yu, 2013, How natalizumab binds and antagonizes α4 integrins, J. Biol. Chem, 288, 32314, 10.1074/jbc.M113.501668 Rose, 2002, α4 integrins and the immune response, Immunol. Rev, 186, 118, 10.1034/j.1600-065X.2002.18611.x Kolaczkowska, 2013, Neutrophil recruitment and function in health and inflammation, Nat. Rev. Immunol, 13, 159, 10.1038/nri3399 Tseng, 2018, Myeloperoxidase negatively regulates neutrophil-endothelial cell interactions by impairing αMβ2 integrin function in sterile inflammation, Front. Med, 5, 134, 10.3389/fmed.2018.00134 Bochner, 1991, Adhesion of human basophils, eosinophils, and neutrophils to interleukin 1-activated human vascular endothelial cells: contributions of endothelial cell adhesion molecules, J. Exp. Med, 173, 1553, 10.1084/jem.173.6.1553 Ibbotson, 2001, Functional α4-integrin: a newly identified pathway of neutrophil recruitment in critically ill septic patients, Nat. Med, 7, 465, 10.1038/86539 Kirveskari, 2000, Expression of α4-integrins on human neutrophils, J. Leukoc. Biol, 68, 243, 10.1189/jlb.68.2.243 Papayannopoulou, 2001, Molecular pathways in bone marrow homing: dominant role of α4β1 over β2-integrins and selectins, Blood, 98, 2403, 10.1182/blood.V98.8.2403 Richter, 2017, Current developments in mobilization of hematopoietic stem and progenitor cells and their interaction with niches in bone marrow, Transfus. Med. Hemother, 44, 151, 10.1159/000477262 Laragione, 2003, Redox regulation of surface protein thiols: identification of integrin α-4 as a molecular target by using redox proteomics, Proc. Natl. Acad. Sci. U.S.A, 100, 14737, 10.1073/pnas.2434516100 Ullevig, 2012, NADPH oxidase 4 mediates monocyte priming and accelerated chemotaxis induced by metabolic stress, Arterioscler. Thromb. Vasc. Biol, 32, 415, 10.1161/ATVBAHA.111.238899 Anathy, 2018, Reducing protein oxidation reverses lung fibrosis, Nat. Med, 24, 1128, 10.1038/s41591-018-0090-y Gorelenkova Miller, 2018, Critical roles of glutaredoxin in brain cells-implications for Parkinson's disease, Antioxid. Redox Signal Yang, 2016, Subinhibitory concentrations of allicin decrease uropathogenic Escherichia coli (UPEC) biofilm formation, adhesion ability, and swimming motility, Int. J. Mol. Sci, 17, E979, 10.3390/ijms17070979