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Volumn 108, Issue 26, 2011, Pages 10650-10655

Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry

Author keywords

[No Author keywords available]

Indexed keywords

BETA3 INTEGRIN; CD4 ANTIGEN; CELL SURFACE PROTEIN; ECALECTIN; GLYCOPROTEIN RECEPTOR; INTEGRIN; LECTIN; PROTEIN DISULFIDE ISOMERASE; UNCLASSIFIED DRUG;

EID: 79960601577     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1017954108     Document Type: Article
Times cited : (197)

References (50)
  • 1
    • 33646698875 scopus 로고    scopus 로고
    • Extracellular disulfide exchange and the regulation of cellular function
    • DOI 10.1089/ars.2006.8.312
    • Jordan PA, Gibbins JM (2006) Extracellular disulfide exchange and the regulation of cellular function. Antioxid Redox Signal 8:312-324. (Pubitemid 43741302)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.3-4 , pp. 312-324
    • Jordan, P.A.1    Gibbins, J.M.2
  • 2
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg PJ (2003) Disulfide bonds as switches for protein function. Trends Biochem Sci 28:210-214.
    • (2003) Trends Biochem Sci , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 3
    • 0029826005 scopus 로고    scopus 로고
    • Surface thiols of human lymphocytes and their changes after in vitro and in vivo activation
    • Lawrence DA, Song R, Weber P (1996) Surface thiols of human lymphocytes and their changes after in vitro and in vivo activation. J Leukoc Biol 60:611-618. (Pubitemid 26400418)
    • (1996) Journal of Leukocyte Biology , vol.60 , Issue.5 , pp. 611-618
    • Lawrence, D.A.1    Song, R.2    Weber, P.3
  • 4
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano C, Coppari S, Altieri F, Ferraro A (2002) Proteins of the PDI family: Unpredicted non-ER locations and functions. J Cell Physiol 193:154-163.
    • (2002) J Cell Physiol , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 5
    • 0035282999 scopus 로고    scopus 로고
    • The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding
    • DOI 10.1086/318823
    • Fenouillet E, Barbouche R, Courageot J, Miquelis R (2001) The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding. J Infect Dis 183:744-752. (Pubitemid 32171749)
    • (2001) Journal of Infectious Diseases , vol.183 , Issue.5 , pp. 744-752
    • Fenouillet, E.1    Barbouche, R.2    Courageot, J.3    Miquelis, R.4
  • 7
    • 0036786353 scopus 로고    scopus 로고
    • Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange
    • Lahav J, et al. (2002) Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange. Blood 100:2472-2478.
    • (2002) Blood , vol.100 , pp. 2472-2478
    • Lahav, J.1
  • 8
    • 33847222149 scopus 로고    scopus 로고
    • Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein
    • Jain S, McGinnes LW, Morrison TG (2007) Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein. J Virol 81:2328-2339.
    • (2007) J Virol , vol.81 , pp. 2328-2339
    • Jain, S.1    McGinnes, L.W.2    Morrison, T.G.3
  • 9
    • 34447502257 scopus 로고    scopus 로고
    • Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus
    • DOI 10.1089/ars.2007.1639
    • Fenouillet E, Barbouche R, Jones IM (2007) Cell entry by enveloped viruses: Redox considerations for HIV and SARS-coronavirus. Antioxid Redox Signal 9:1009-1034. (Pubitemid 47080818)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.8 , pp. 1009-1034
    • Fenouillet, E.1    Barbouche, R.2    Jones, I.M.3
  • 13
    • 77951530547 scopus 로고    scopus 로고
    • Mapping of domains on HIV envelope protein mediating association with calnexin and protein-disulfide isomerase
    • Papandréou MJ, et al. (2010) Mapping of domains on HIV envelope protein mediating association with calnexin and protein-disulfide isomerase. J Biol Chem 285:13788-13796.
    • (2010) J Biol Chem , vol.285 , pp. 13788-13796
    • Papandréou, M.J.1
  • 14
    • 75749101401 scopus 로고    scopus 로고
    • Galectins: Regulators of acute and chronic inflammation
    • Liu F-T, Rabinovich GA (2010) Galectins: Regulators of acute and chronic inflammation. Ann N Y Acad Sci 1183:158-182.
    • (2010) Ann N Y Acad Sci , vol.1183 , pp. 158-182
    • Liu, F.-T.1    Rabinovich, G.A.2
  • 15
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • Vasta GR (2009) Roles of galectins in infection. Nat Rev Microbiol 7:424-438.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 16
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling
    • Garner OB, Baum LG (2008) Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem Soc Trans 36:1472-1477.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 17
    • 45549107987 scopus 로고    scopus 로고
    • Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways
    • Bi S, Earl LA, Jacobs L, Baum LG (2008) Structural features of galectin-9 and galectin-1 that determine distinct T cell death pathways. J Biol Chem 283:12248-12258.
    • (2008) J Biol Chem , vol.283 , pp. 12248-12258
    • Bi, S.1    Earl, L.A.2    Jacobs, L.3    Baum, L.G.4
  • 19
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-Glycan Number and Degree of Branching Cooperate to Regulate Cell Proliferation and Differentiation
    • DOI 10.1016/j.cell.2007.01.049, PII S0092867407003157
    • Lau KS, et al. (2007) Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell 129:123-134. (Pubitemid 46507588)
    • (2007) Cell , vol.129 , Issue.1 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3    Silvescu, C.I.4    Reinhold, V.N.5    Demetriou, M.6    Dennis, J.W.7
  • 20
    • 67649781736 scopus 로고    scopus 로고
    • T-cell growth, cell surface organization, and the galectin-glycoprotein lattice
    • Grigorian A, Torossian S, Demetriou M (2009) T-cell growth, cell surface organization, and the galectin-glycoprotein lattice. Immunol Rev 230:232-246.
    • (2009) Immunol Rev , vol.230 , pp. 232-246
    • Grigorian, A.1    Torossian, S.2    Demetriou, M.3
  • 21
    • 77449124815 scopus 로고    scopus 로고
    • N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death
    • Earl LA, Bi S, Baum LG (2010) N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. J Biol Chem 285:2232-2244.
    • (2010) J Biol Chem , vol.285 , pp. 2232-2244
    • Earl, L.A.1    Bi, S.2    Baum, L.G.3
  • 24
    • 34547099820 scopus 로고    scopus 로고
    • Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death
    • Toscano MA, et al. (2007) Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death. Nat Immunol 8:825-834.
    • (2007) Nat Immunol , vol.8 , pp. 825-834
    • Toscano, M.A.1
  • 25
    • 33646857224 scopus 로고    scopus 로고
    • Endothelial cell expression of galectin-1 induced by prostate cancer cells inhibits T-cell transendothelial migration
    • DOI 10.1038/labinvest.3700420, PII 3700420
    • He J, Baum LG (2006) Endothelial cell expression of galectin-1 induced by prostate cancer cells inhibits T-cell transendothelial migration. Lab Invest 86:578-590. (Pubitemid 43780439)
    • (2006) Laboratory Investigation , vol.86 , Issue.6 , pp. 578-590
    • He, J.1    Baum, L.G.2
  • 28
    • 0034674762 scopus 로고    scopus 로고
    • Protein disulfide isomerase mediates integrin-dependent adhesion
    • DOI 10.1016/S0014-5793(00)01630-6, PII S0014579300016306
    • Lahav J, Gofer-Dadosh N, Luboshitz J, Hess O, Shaklai M (2000) Protein disulfide isomerase mediates integrin-dependent adhesion. FEBS Lett 475:89-92. (Pubitemid 30365056)
    • (2000) FEBS Letters , vol.475 , Issue.2 , pp. 89-92
    • Lahav, J.1    Gofer-Dadosh, N.2    Luboshitz, J.3    Hess, O.4    Shaklai, M.5
  • 29
    • 77956919583 scopus 로고    scopus 로고
    • Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3
    • Swiatkowska M, et al. (2010) Ero1alpha is expressed on blood platelets in association with protein-disulfide isomerase and contributes to redox-controlled remodeling of alphaIIbbeta3. J Biol Chem 285:29874-29883.
    • (2010) J Biol Chem , vol.285 , pp. 29874-29883
    • Swiatkowska, M.1
  • 30
    • 36148955067 scopus 로고    scopus 로고
    • Myelin basic protein-primed T cells induce neurotrophins in glial cells via alpha5beta3 integrin
    • DOI 10.1074/jbc.M702899200
    • Roy A, Liu X, Pahan K (2007) Myelin basic protein-primed T cells induce neurotrophins in glial cells via alphavbeta3 [corrected] integrin. J Biol Chem 282:32222-32232. (Pubitemid 350106469)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.44 , pp. 32222-32232
    • Roy, A.1    Liu, X.2    Pahan, K.3
  • 33
    • 33644533855 scopus 로고    scopus 로고
    • Beta 3 integrin expression on T cells from renal allograft recipients
    • Wierzbicki P, et al. (2006) Beta 3 integrin expression on T cells from renal allograft recipients. Transplant Proc 38:338-339.
    • (2006) Transplant Proc , vol.38 , pp. 338-339
    • Wierzbicki, P.1
  • 34
    • 0038035145 scopus 로고    scopus 로고
    • The beta1 and beta3 integrins promote T cell receptor-mediated cytotoxic T lymphocyte activation
    • Doucey MA, et al. (2003) The beta1 and beta3 integrins promote T cell receptor-mediated cytotoxic T lymphocyte activation. J Biol Chem 278:26983-26991.
    • (2003) J Biol Chem , vol.278 , pp. 26983-26991
    • Doucey, M.A.1
  • 36
    • 78649462789 scopus 로고    scopus 로고
    • Reduced monomeric CD4 is the preferred receptor for HIV
    • Matthias LJ, Azimi I, Tabrett CA, Hogg PJ (2010) Reduced monomeric CD4 is the preferred receptor for HIV. J Biol Chem 285:40793-40799.
    • (2010) J Biol Chem , vol.285 , pp. 40793-40799
    • Matthias, L.J.1    Azimi, I.2    Tabrett, C.A.3    Hogg, P.J.4
  • 38
    • 18644386263 scopus 로고    scopus 로고
    • Interferon-gamma stimulates the expression of galectin-9 in cultured human endothelial cells
    • Imaizumi T, et al. (2002) Interferon-gamma stimulates the expression of galectin-9 in cultured human endothelial cells. J Leukoc Biol 72:486-491.
    • (2002) J Leukoc Biol , vol.72 , pp. 486-491
    • Imaizumi, T.1
  • 39
    • 77954902619 scopus 로고    scopus 로고
    • Thiol isomerases negatively regulate the cellular shedding activity of ADAM17
    • Willems SH, et al. (2010) Thiol isomerases negatively regulate the cellular shedding activity of ADAM17. Biochem J 428:439-450.
    • (2010) Biochem J , vol.428 , pp. 439-450
    • Willems, S.H.1
  • 40
    • 57649166525 scopus 로고    scopus 로고
    • Molecular docking studies of dithionitrobenzoic acid and its related compounds to protein disulfide isomerase: Computational screening of inhibitors to HIV-1 entry
    • Gowthaman U, Jayakanthan M, Sundar D (2008) Molecular docking studies of dithionitrobenzoic acid and its related compounds to protein disulfide isomerase: Computational screening of inhibitors to HIV-1 entry. BMC Bioinformatics 9(Suppl 12):S14.
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPPL. 12
    • Gowthaman, U.1    Jayakanthan, M.2    Sundar, D.3
  • 41
    • 79251589403 scopus 로고    scopus 로고
    • Galectin multimerization and lattice formation are regulated by linker region structure
    • Earl LA, Bi S, Baum LG (2011) Galectin multimerization and lattice formation are regulated by linker region structure. Glycobiology 21:6-12.
    • (2011) Glycobiology , vol.21 , pp. 6-12
    • Earl, L.A.1    Bi, S.2    Baum, L.G.3
  • 42
    • 70350163821 scopus 로고    scopus 로고
    • Galectin-9 in allergic airway inflammation and hyperresponsiveness in mice
    • Sziksz E, et al. (2010) Galectin-9 in allergic airway inflammation and hyperresponsiveness in mice. Int Arch Allergy Immunol 151:308-317.
    • (2010) Int Arch Allergy Immunol , vol.151 , pp. 308-317
    • Sziksz, E.1
  • 43
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • DOI 10.1016/j.cell.2005.09.041, PII S0092867405011712
    • Ohtsubo K, et al. (2005) Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes. Cell 123:1307-1321. (Pubitemid 41821787)
    • (2005) Cell , vol.123 , Issue.7 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3    Yoshida, A.4    Takeuchi, M.5    Marth, J.D.6
  • 44
    • 78049312395 scopus 로고    scopus 로고
    • Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells
    • Mishra R, Grzybek M, Niki T, Hirashima M, Simons K (2010) Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells. Proc Natl Acad Sci USA 107:17633-17638.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17633-17638
    • Mishra, R.1    Grzybek, M.2    Niki, T.3    Hirashima, M.4    Simons, K.5
  • 45
    • 0142075256 scopus 로고    scopus 로고
    • Preparation of recombinant human Galectin-1 and use in T-cell death assays
    • DOI 10.1016/S0076-6879(03)01075-9
    • Pace KE, Hahn HP, Baum LG (2003) Preparation of recombinant human galectin-1 and use in T-cell death assays. Methods Enzymol 363:499-518. (Pubitemid 37267694)
    • (2003) Methods in Enzymology , vol.363 , pp. 499-518
    • Pace, K.E.1    Hahn, H.P.2    Baum, L.G.3
  • 46
  • 48
    • 0035913944 scopus 로고    scopus 로고
    • CCR5 and CXCR4 expression correlated with X4 and R5 HIV-1 infection yet not sustained replication in Th1 and Th2 cells
    • DOI 10.1097/00002030-200110190-00005
    • Moonis M, Lee B, Bailer RT, Luo Q, Montaner LJ (2001) CCR5 and CXCR4 expression correlated with X4 and R5 HIV-1 infection yet not sustained replication in Th1 and Th2 cells. AIDS 15:1941-1949. (Pubitemid 32980635)
    • (2001) AIDS , vol.15 , Issue.15 , pp. 1941-1949
    • Moonis, M.1    Lee, B.2    Bailer, R.T.3    Luo, Q.4    Montaner, L.J.5
  • 50
    • 34547127164 scopus 로고    scopus 로고
    • Identification of the optimal DC-SIGN binding site on human immunodeficiency virus type 1 gp120
    • DOI 10.1128/JVI.01765-06
    • Hong PW, Nguyen S, Young S, Su SV, Lee B (2007) Identification of the optimal DCSIGN binding site on human immunodeficiency virus type 1 gp120. J Virol 81:8325-8336. (Pubitemid 47101517)
    • (2007) Journal of Virology , vol.81 , Issue.15 , pp. 8325-8336
    • Hong, P.W.-P.1    Nguyen, S.2    Young, S.3    Su, S.V.4    Lee, B.5


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