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Volumn 183, Issue 12, 2009, Pages 7703-7709

Siglec-E is up-regulated and phosphorylated following lipopolysaccharide stimulation in order to limit TLR-driven cytokine production

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LECTIN RECEPTOR; LIPOPOLYSACCHARIDE; MYELOID DIFFERENTIATION FACTOR 88; PROTEIN TYROSINE PHOSPHATASE SHP 2; RANTES; SIGLEC E; TOLL LIKE RECEPTOR; TYROSINE; UNCLASSIFIED DRUG; B LYMPHOCYTE ANTIGEN; CYTOKINE; LEUKOCYTE ANTIGEN; MYD88 PROTEIN, MOUSE; PTPN11 PROTEIN, MOUSE; SIGLEC E ANTIGEN, MOUSE; SIGLEC-E ANTIGEN, MOUSE; TICAM 1 PROTEIN, MOUSE; TICAM-1 PROTEIN, MOUSE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 76249093445     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0902780     Document Type: Article
Times cited : (65)

References (34)
  • 1
    • 55449136389 scopus 로고    scopus 로고
    • Innate microbial sensors and their relevance to allergy
    • quiz 858-860
    • Liu, A. H. 2008. Innate microbial sensors and their relevance to allergy. J. Allergy Clin. Immunol. 122: 846-858; quiz 858-860.
    • (2008) J. Allergy Clin. Immunol. , vol.122 , pp. 846-858
    • Liu, A.H.1
  • 2
    • 51349158231 scopus 로고    scopus 로고
    • Signalling adaptors used by Toll-like receptors: An update
    • Kenny, E. F., and L. A. O'Neill. 2008. Signalling adaptors used by Toll-like receptors: an update. Cytokine 43: 342-349.
    • (2008) Cytokine , vol.43 , pp. 342-349
    • Kenny, E.F.1    O'Neill, L.A.2
  • 3
    • 0037178785 scopus 로고    scopus 로고
    • IRAK-M is a negative regulator of Toll-like receptor signaling
    • DOI 10.1016/S0092-8674(02)00827-9
    • Kobayashi, K., L. D. Hernandez, J. E. Galan, C. A. Janeway, Jr., R. Medzhitov, and R. A. Flavell. 2002. IRAK-M is a negative regulator of Toll-like receptor signaling. Cell 110: 191-202. (Pubitemid 34876547)
    • (2002) Cell , vol.110 , Issue.2 , pp. 191-202
    • Kobayashi, K.1    Hernandez, L.D.2    Galan, J.E.3    Janeway Jr., C.A.4    Medzhitov, R.5    Flavell, R.A.6
  • 4
    • 0037454946 scopus 로고    scopus 로고
    • Inhibition of interleukin 1 receptor/toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4
    • DOI 10.1084/jem.20021790
    • Burns, K., S. Janssens, B. Brissoni, N. Olivos, R. Beyaert, and J. Tschopp. 2003. Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4. J. Exp. Med. 197: 263-268. (Pubitemid 36152320)
    • (2003) Journal of Experimental Medicine , vol.197 , Issue.2 , pp. 263-268
    • Burns, K.1    Janssens, S.2    Brissoni, B.3    Olivos, N.4    Beyaert, R.5    Tschopp, J.6
  • 5
    • 40949163764 scopus 로고    scopus 로고
    • TRIM30α negatively regulates TLR-mediated NF-κB activation by targeting TAB2 and TAB3 for degradation
    • DOI 10.1038/ni1577, PII NI1577
    • Shi, M., W. Deng, E. Bi, K. Mao, Y. Ji, G. Lin, X. Wu, Z. Tao, Z. Li, X. Cai, et al. 2008. TRIM30 α negatively regulates TLR-mediated NF-κB activation by targeting TAB2 and TAB3 for degradation. Nat. Immunol. 9: 369-377. (Pubitemid 351405106)
    • (2008) Nature Immunology , vol.9 , Issue.4 , pp. 369-377
    • Shi, M.1    Deng, W.2    Bi, E.3    Mao, K.4    Ji, Y.5    Lin, G.6    Wu, X.7    Tao, Z.8    Li, Z.9    Cai, X.10    Sun, S.11    Xiang, C.12    Sun, B.13
  • 6
    • 33748871187 scopus 로고    scopus 로고
    • The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling
    • DOI 10.1038/ni1382, PII NI1382
    • Carty, M., R. Goodbody, M. Schroder, J. Stack, P. N. Moynagh, and A. G. Bowie. 2006. The human adaptor SARM negatively regulates adaptor protein TRIF-dependent Toll-like receptor signaling. Nat. Immunol. 7: 1074-1081. (Pubitemid 44420652)
    • (2006) Nature Immunology , vol.7 , Issue.10 , pp. 1074-1081
    • Carty, M.1    Goodbody, R.2    Schroder, M.3    Stack, J.4    Moynagh, P.N.5    Bowie, A.G.6
  • 7
    • 49649125136 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Ro52 negatively regulates IFN-β production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3
    • Higgs, R., J. Ni Gabhann, N. Ben Larbi, E. P. Breen, K. A. Fitzgerald, and C. A. Jefferies. 2008. The E3 ubiquitin ligase Ro52 negatively regulates IFN-β production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. J. Immunol. 181: 1780-1786.
    • (2008) J. Immunol. , vol.181 , pp. 1780-1786
    • Higgs, R.1    Ni Gabhann, J.2    Ben Larbi, N.3    Breen, E.P.4    Fitzgerald, K.A.5    Jefferies, C.A.6
  • 9
    • 46749119743 scopus 로고    scopus 로고
    • Phosphatase PTP1B negatively regulates MyD88- And TRIF-dependent proinflammatory cytokine and type I interferon production in TLR-triggered macrophages
    • Xu, H., H. An, J. Hou, C. Han, P. Wang, Y. Yu, and X. Cao. 2008. Phosphatase PTP1B negatively regulates MyD88- and TRIF-dependent proinflammatory cytokine and type I interferon production in TLR-triggered macrophages. Mol. Immunol. 45: 3545-3552.
    • (2008) Mol. Immunol. , vol.45 , pp. 3545-3552
    • Xu, H.1    An, H.2    Hou, J.3    Han, C.4    Wang, P.5    Yu, Y.6    Cao, X.7
  • 11
    • 33846864687 scopus 로고    scopus 로고
    • CD33 responses are blocked by SOCS3 through accelerated proteasomal-mediated turnover
    • Orr, S. J., N. M. Morgan, J. Elliott, J. F. Burrows, C. J. Scott, D. W. McVicar, and J. A. Johnston. 2007. CD33 responses are blocked by SOCS3 through accelerated proteasomal-mediated turnover. Blood 109: 1061-1068.
    • (2007) Blood , vol.109 , pp. 1061-1068
    • Orr, S.J.1    Morgan, N.M.2    Elliott, J.3    Burrows, J.F.4    Scott, C.J.5    McVicar, D.W.6    Johnston, J.A.7
  • 12
    • 34248376987 scopus 로고    scopus 로고
    • Defining the in vivo function of Siglec-F, a CD33-related Siglec expressed on mouse eosinophils
    • DOI 10.1182/blood-2006-08-039255
    • Zhang, M., T. Angata, J. Y. Cho, M. Miller, D. H. Broide, and A. Varki. 2007. Defining the in vivo function of Siglec-F, a CD33-related Siglec expressed on mouse eosinophils. Blood 109: 4280-4287. (Pubitemid 46743394)
    • (2007) Blood , vol.109 , Issue.10 , pp. 4280-4287
    • Zhang, M.1    Angata, T.2    Jae, Y.C.3    Miller, M.4    Broide, D.H.5    Varki, A.6
  • 14
    • 41649097373 scopus 로고    scopus 로고
    • Siglecg limits the size of B1a B cell lineage by down-regulating NFκB activation
    • DOI 10.1371/journal.pone.0000997
    • Ding, C., Y. Liu, Y. Wang, B. K. Park, C. Y. Wang, P. Zheng, and Y. Liu. 2007. Siglecg limits the size of B1a B cell lineage by down-regulating NFκB activation. PLoS ONE 2(10): e997. (Pubitemid 351479820)
    • (2007) PLoS ONE , vol.2 , Issue.10
    • Ding, C.1    Liu, Y.2    Wang, Y.3    Park, B.K.4    Wang, C.-Y.5    Zheng, P.6    Liu, Y.7
  • 15
    • 41149114476 scopus 로고    scopus 로고
    • Siglec-9 enhances IL-10 production in macrophages via tyrosine-based motifs
    • Ando, M., W. Tu, K. Nishijima, and S. Iijima. 2008. Siglec-9 enhances IL-10 production in macrophages via tyrosine-based motifs. Biochem. Biophys. Res. Commun. 369: 878-883.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 878-883
    • Ando, M.1    Tu, W.2    Nishijima, K.3    Iijima, S.4
  • 16
    • 3843145244 scopus 로고    scopus 로고
    • The murine inhibitory receptor mSiglec-E is expressed broadly on cells of the innate immune system whereas mSiglec-F is restricted to eosinophils
    • Zhang, J. Q., B. Biedermann, L. Nitschke, and P. R. Crocker. 2004. The murine inhibitory receptor mSiglec-E is expressed broadly on cells of the innate immune system whereas mSiglec-F is restricted to eosinophils. Eur. J. Immunol. 34: 1175-1184.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 1175-1184
    • Zhang, J.Q.1    Biedermann, B.2    Nitschke, L.3    Crocker, P.R.4
  • 19
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • Crocker, P. R., J. C. Paulson, and A. Varki. 2007. Siglecs and their roles in the immune system. Nat. Rev. Immunol. 7: 255-266.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 22
    • 0035957935 scopus 로고    scopus 로고
    • Molecular Cloning of MIS, a Myeloid Inhibitory Siglec, That Binds Protein-tyrosine Phosphatases SHP-1 and SHP-2
    • Ulyanova, T., D. D. Shah, and M. L. Thomas. 2001. Molecular cloning of MIS, a myeloid inhibitory siglec, that binds protein-tyrosine phosphatases SHP-1 and SHP-2. J. Biol. Chem. 276: 14451-14458. (Pubitemid 37391838)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.17 , pp. 14451-14458
    • Ulyanova, T.1    Shah, D.D.2    Thomas, M.L.3
  • 23
    • 0035252999 scopus 로고    scopus 로고
    • MSiglec-E, a novel mouse CD33-related siglec (sialic acid-binding immunoglobulin-like lectin) that recruits Src homology 2 (SH2)-domain-containing protein tyrosine phosphatases SHP-1 and SHP-2
    • DOI 10.1042/0264-6021:3530483
    • Yu, Z., M. Maoui, L. Wu, D. Banville, and S. Shen. 2001. mSiglec-E, a novel mouse CD33-related siglec (sialic acid-binding immunoglobulin-like lectin) that recruits Src homology 2 (SH2)-domain-containing protein tyrosine phosphatases SHP-1 and SHP-2. Biochem. J. 353: 483-492. (Pubitemid 32158316)
    • (2001) Biochemical Journal , vol.353 , Issue.3 , pp. 483-492
    • Yu, Z.1    Maoui, M.2    Wu, L.3    Banville, D.4    Shen, S.-H.5
  • 24
    • 33644548670 scopus 로고    scopus 로고
    • SHP2 forecast for the immune system: Fog gradually clearing
    • DOI 10.1016/j.it.2006.01.007, PII S1471490606000251
    • Salmond, R. J., and D. R. Alexander. 2006. SHP2 forecast for the immune system: fog gradually clearing. Trends Immunol. 27: 154-160. (Pubitemid 43306810)
    • (2006) Trends in Immunology , vol.27 , Issue.3 , pp. 154-160
    • Salmond, R.J.1    Alexander, D.R.2
  • 25
    • 23944518951 scopus 로고    scopus 로고
    • A SHPing tale: Perspectives on the regulation of SHP-1 and SHP-2 tyrosine phosphatases by the C-terminal tail
    • Poole, A. W., and M. L. Jones. 2005. A SHPing tale: perspectives on the regulation of SHP-1 and SHP-2 tyrosine phosphatases by the C-terminal tail. Cell Signal 17: 1323-1332.
    • (2005) Cell Signal , vol.17 , pp. 1323-1332
    • Poole, A.W.1    Jones, M.L.2
  • 26
    • 33845438110 scopus 로고    scopus 로고
    • SHP-2 Phosphatase Negatively Regulates the TRIF Adaptor Protein-Dependent Type I Interferon and Proinflammatory Cytokine Production
    • DOI 10.1016/j.immuni.2006.10.014, PII S1074761306005127
    • An, H., W. Zhao, J. Hou, Y. Zhang, Y. Xie, Y. Zheng, H. Xu, C. Qian, J. Zhou, Y. Yu, et al. 2006. SHP-2 phosphatase negatively regulates the TRIF adaptor protein-dependent type I interferon and proinflammatory cytokine production. Immunity 25: 919-928. (Pubitemid 44894946)
    • (2006) Immunity , vol.25 , Issue.6 , pp. 919-928
    • An, H.1    Zhao, W.2    Hou, J.3    Zhang, Y.4    Xie, Y.5    Zheng, Y.6    Xu, H.7    Qian, C.8    Zhou, J.9    Yu, Y.10    Liu, S.11    Feng, G.12    Cao, X.13
  • 27
    • 42449121356 scopus 로고    scopus 로고
    • Phosphatase SHP-1 promotes TLR- And RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1
    • DOI 10.1038/ni.1604, PII NI.1604
    • An, H., J. Hou, J. Zhou, W. Zhao, H. Xu, Y. Zheng, Y. Yu, S. Liu, and X. Cao. 2008. Phosphatase SHP-1 promotes TLR- and RIG-I-activated production of type I interferon by inhibiting the kinase IRAK1. Nat. Immunol. 9: 542-550. (Pubitemid 351560523)
    • (2008) Nature Immunology , vol.9 , Issue.5 , pp. 542-550
    • An, H.1    Hou, J.2    Zhou, J.3    Zhao, W.4    Xu, H.5    Zheng, Y.6    Yu, Y.7    Liu, S.8    Cao, X.9
  • 29
    • 2942721674 scopus 로고    scopus 로고
    • ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance
    • Brint, E. K., D. Xu, H. Liu, A. Dunne, A. N. McKenzie, L. A. O'Neill, and F. Y. Liew. 2004. ST2 is an inhibitor of interleukin 1 receptor and Toll-like receptor 4 signaling and maintains endotoxin tolerance. Nat. Immunol. 5: 373-379.
    • (2004) Nat. Immunol. , vol.5 , pp. 373-379
    • Brint, E.K.1    Xu, D.2    Liu, H.3    Dunne, A.4    McKenzie, A.N.5    O'Neill, L.A.6    Liew, F.Y.7
  • 32
    • 41249084567 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of MyD88 adapter-like (Mal) is critical for signal transduction and blocked in endotoxin tolerance
    • Piao, W., C. Song, H. Chen, L. M. Wahl, K. A. Fitzgerald, L. A. O'Neill, and A. E. Medvedev. 2008. Tyrosine phosphorylation of MyD88 adapter-like (Mal) is critical for signal transduction and blocked in endotoxin tolerance. J. Biol. Chem. 283: 3109-3119.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3109-3119
    • Piao, W.1    Song, C.2    Chen, H.3    Wahl, L.M.4    Fitzgerald, K.A.5    O'Neill, L.A.6    Medvedev, A.E.7
  • 33
    • 0037492123 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is a Toll/interleukin-1 receptor domain-binding protein that participates in nuclear factor κB activation by Toll-like receptor 4
    • Jefferies, C. A., S. Doyle, C. Brunner, A. Dunne, E. Brint, C. Wietek, E. Walch, T. Wirth, and L. A. O'Neill. 2003. Bruton's tyrosine kinase is a Toll/interleukin-1 receptor domain-binding protein that participates in nuclear factor κB activation by Toll-like receptor 4. J. Biol. Chem. 278: 26258-26264.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26258-26264
    • Jefferies, C.A.1    Doyle, S.2    Brunner, C.3    Dunne, A.4    Brint, E.5    Wietek, C.6    Walch, E.7    Wirth, T.8    O'Neill, L.A.9


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