The protease cathepsin L regulates Th17 cell differentiation

Journal of Autoimmunity - Tập 65 - Trang 56-63 - 2015
Lifei Hou1,2, Jessica Cooley1, Richard Swanson3, Poh Chee Ong4, Robert N. Pike4, Matthew Bogyo5, Steven T. Olson3, Eileen Remold-O’Donnell1,6,2
1Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA
2Department of Pediatrics, Harvard Medical School, Boston, MA 02115, USA
3Department of Periodontics, University of Illinois at Chicago, Chicago, IL 60612, USA
4Department of Biochemistry and Molecular Biology, Monash University, Clayton VIC 3800, Australia
5Department of Pathology, Stanford University School of Medicine, Palo Alto, CA 94305, USA
6Division of Hematology/Oncology, Boston Children’s Hospital, Boston, MA 02115, USA

Tài liệu tham khảo

Harrington, 2005, Interleukin 17-producing CD4+ effector T cells develop via a lineage distinct from the T helper type 1 and 2 lineages, Nat. Immunol., 6, 1123, 10.1038/ni1254 Park, 2005, A distinct lineage of CD4 T cells regulates tissue inflammation by producing interleukin 17, Nat. Immunol., 6, 1133, 10.1038/ni1261 Bettelli, 2006, Reciprocal developmental pathways for the generation of pathogenic effector TH17 and regulatory T cells, Nature, 441, 235, 10.1038/nature04753 Mangan, 2006, Transforming growth factor-beta induces development of the T(H)17 lineage, Nature, 441, 231, 10.1038/nature04754 Zhou, 2007, IL-6 programs T(H)-17 cell differentiation by promoting sequential engagement of the IL-21 and IL-23 pathways, Nat. Immunol., 8, 967, 10.1038/ni1488 Durant, 2010, Diverse targets of the transcription factor STAT3 contribute to T cell pathogenicity and homeostasis, Immunity, 32, 605, 10.1016/j.immuni.2010.05.003 Ivanov, 2006, The orphan nuclear receptor RORgammat directs the differentiation program of proinflammatory IL-17+ T helper cells, Cell, 126, 1121, 10.1016/j.cell.2006.07.035 McGeachy, 2009, The interleukin 23 receptor is essential for the terminal differentiation of interleukin 17-producing effector T helper cells in vivo, Nat. Immunol., 10, 314, 10.1038/ni.1698 Ciofani, 2012, A validated regulatory network for Th17 cell specification, Cell, 151, 289, 10.1016/j.cell.2012.09.016 Yosef, 2013, Dynamic regulatory network controlling TH17 cell differentiation, Nature, 496, 461, 10.1038/nature11981 Gong, 2011, Critical role of serpinB1 in regulating inflammatory responses in pulmonary influenza infection, J. Infect. Dis., 204, 592, 10.1093/infdis/jir352 Zhao, 2014, SerpinB1 regulates homeostatic expansion of IL-17+ gammadelta and CD4+ Th17 cells, J. Leukoc. Biol., 95, 521, 10.1189/jlb.0613331 Benarafa, 2007, The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in Pseudomonas aeruginosa infection, J. Exp. Med., 204, 1901, 10.1084/jem.20070494 Buhling, 2011, Gene targeting of the cysteine peptidase cathepsin H impairs lung surfactant in mice, PloS one, 6, e26247, 10.1371/journal.pone.0026247 Lee, 2012, Synthesis and evaluation of aza-peptidyl inhibitors of the lysosomal asparaginyl endopeptidase, legumain, Bioorg. Med. Chem. Lett., 22, 1340, 10.1016/j.bmcl.2011.12.079 Greenbaum, 2000, Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools, Chem. Biol., 7, 569, 10.1016/S1074-5521(00)00014-4 Shi, 2000, Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages, J. Exp. Med., 191, 1177, 10.1084/jem.191.7.1177 Zhou, 2008, TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by antagonizing RORgammat function, Nature, 453, 236, 10.1038/nature06878 Barrett, 1982, L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L, Biochem. J., 201, 189, 10.1042/bj2010189 Cooley, 2001, The serpin MNEI inhibits elastase-like and chymotrypsin-like serine proteases through efficient reactions at two active sites, Biochemistry, 40, 15762, 10.1021/bi0113925 Silverman, 2001, The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature, J. Biol. Chem., 276, 33293, 10.1074/jbc.R100016200 Reiser, 2010, Specialized roles for cysteine cathepsins in health and disease, J. Clin. Invest., 120, 3421, 10.1172/JCI42918 Gettins, 2002, Serpin structure, mechanism, and function, Chem. Rev., 102, 4751, 10.1021/cr010170+ Nakagawa, 1999, The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation, Immunol. Rev., 172, 121, 10.1111/j.1600-065X.1999.tb01361.x Drake, 1996, Cathepsin K, but not cathepsins B, L, or S, is abundantly expressed in human osteoclasts, J. Biol. Chem., 271, 12511, 10.1074/jbc.271.21.12511 Katunuma, 1999, Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo, FEBS Lett., 458, 6, 10.1016/S0014-5793(99)01107-2 Yasuma, 1998, Synthesis of peptide aldehyde derivatives as selective inhibitors of human cathepsin L and their inhibitory effect on bone resorption, J. Med. Chem., 41, 4301, 10.1021/jm9803065 Liszewski, 2013, Intracellular complement activation sustains T cell homeostasis and mediates effector differentiation, Immunity, 39, 1143, 10.1016/j.immuni.2013.10.018 Tuomela, 2012, Identification of early gene expression changes during human Th17 cell differentiation, Blood, 119, e151, 10.1182/blood-2012-01-407528 Shirahama-Noda, 2003, Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice, J. Biol. Chem., 278, 33194, 10.1074/jbc.M302742200 Maehr, 2005, Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice, J. Immunol., 174, 7066, 10.4049/jimmunol.174.11.7066