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Volumn 1820, Issue 7, 2012, Pages 804-818

Galectin-3 endocytosis by carbohydrate independent and dependent pathways in different macrophage like cell types

Author keywords

Endocytosis; Galectin 3; M1 macrophages; M2 macrophages; THP 1 cell line

Indexed keywords

ARGININE; CARBOHYDRATE; CHLORPROMAZINE; GALECTIN 3; LACTOSE; MUTANT PROTEIN; PROTEIN INHIBITOR; SERINE;

EID: 84860675027     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.02.018     Document Type: Article
Times cited : (52)

References (66)
  • 1
    • 54449093241 scopus 로고    scopus 로고
    • Differentiation and heterogeneity in the mononuclear phagocyte system
    • D.A. Hume Differentiation and heterogeneity in the mononuclear phagocyte system Mucosal Immunol. 1 2008 432 441
    • (2008) Mucosal Immunol. , vol.1 , pp. 432-441
    • Hume, D.A.1
  • 2
    • 30044434256 scopus 로고    scopus 로고
    • The mononuclear phagocyte system
    • D.A. Hume The mononuclear phagocyte system Curr. Opin. Immunol. 18 2006 49 53
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 49-53
    • Hume, D.A.1
  • 3
    • 0024221476 scopus 로고
    • Structural and functional aspects of Kupffer cells
    • L. Bouwens Structural and functional aspects of Kupffer cells Revisiones sobre biologia celular: RBC 16 1988 69 94
    • (1988) Revisiones Sobre Biologia Celular: RBC , vol.16 , pp. 69-94
    • Bouwens, L.1
  • 4
    • 77953268611 scopus 로고    scopus 로고
    • Alternative activation of macrophages: Mechanism and functions
    • S. Gordon, and F.O. Martinez Alternative activation of macrophages: mechanism and functions Immunity 32 2010 593 604
    • (2010) Immunity , vol.32 , pp. 593-604
    • Gordon, S.1    Martinez, F.O.2
  • 5
    • 67650485985 scopus 로고    scopus 로고
    • Alternative activation of macrophages: An immunologic functional perspective
    • F.O. Martinez, L. Helming, and S. Gordon Alternative activation of macrophages: an immunologic functional perspective Annu. Rev. Immunol. 27 2009 451 483
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 451-483
    • Martinez, F.O.1    Helming, L.2    Gordon, S.3
  • 7
    • 0028874589 scopus 로고
    • Expression and function of galectin-3, a beta-galactoside-binding lectin, in human monocytes and macrophages
    • F.T. Liu, D.K. Hsu, R.I. Zuberi, I. Kuwabara, E.Y. Chi, and W.R. Henderson Jr. Expression and function of galectin-3, a beta-galactoside-binding lectin, in human monocytes and macrophages Am. J. Pathol. 147 1995 1016 1028
    • (1995) Am. J. Pathol. , vol.147 , pp. 1016-1028
    • Liu, F.T.1    Hsu, D.K.2    Zuberi, R.I.3    Kuwabara, I.4    Chi, E.Y.5    Henderson, Jr.W.R.6
  • 8
    • 74149092361 scopus 로고    scopus 로고
    • The role of galectin-3/MAC-2 in the activation of the innate-immune function of phagocytosis in microglia in injury and disease
    • S. Rotshenker The role of galectin-3/MAC-2 in the activation of the innate-immune function of phagocytosis in microglia in injury and disease J. Mol. Neurosci. 39 2009 99 103
    • (2009) J. Mol. Neurosci. , vol.39 , pp. 99-103
    • Rotshenker, S.1
  • 9
    • 0020058758 scopus 로고
    • Mac-2, a novel 32,000 Mr mouse macrophage subpopulation-specific antigen defined by monoclonal antibodies
    • M.K. Ho, and T.A. Springer Mac-2, a novel 32,000 Mr mouse macrophage subpopulation-specific antigen defined by monoclonal antibodies J. Immunol. 128 1982 1221 1228
    • (1982) J. Immunol. , vol.128 , pp. 1221-1228
    • Ho, M.K.1    Springer, T.A.2
  • 11
    • 0030707480 scopus 로고    scopus 로고
    • Galectin-3: A novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family
    • S. Akahani, P. Nangia-Makker, H. Inohara, H.R. Kim, and A. Raz Galectin-3: a novel antiapoptotic molecule with a functional BH1 (NWGR) domain of Bcl-2 family Cancer Res. 57 1997 5272 5276
    • (1997) Cancer Res. , vol.57 , pp. 5272-5276
    • Akahani, S.1    Nangia-Makker, P.2    Inohara, H.3    Kim, H.R.4    Raz, A.5
  • 12
    • 23844534708 scopus 로고    scopus 로고
    • Galectin-3 regulates a molecular switch from N-Ras to K-Ras usage in human breast carcinoma cells
    • R. Shalom-Feuerstein, T. Cooks, A. Raz, and Y. Kloog Galectin-3 regulates a molecular switch from N-Ras to K-Ras usage in human breast carcinoma cells Cancer Res. 65 2005 7292 7300
    • (2005) Cancer Res. , vol.65 , pp. 7292-7300
    • Shalom-Feuerstein, R.1    Cooks, T.2    Raz, A.3    Kloog, Y.4
  • 13
    • 60549098654 scopus 로고    scopus 로고
    • Galectin-3 mediates nuclear beta-catenin accumulation and Wnt signaling in human colon cancer cells by regulation of glycogen synthase kinase-3beta activity
    • S. Song, N. Mazurek, C. Liu, Y. Sun, Q.Q. Ding, K. Liu, M.C. Hung, and R.S. Bresalier Galectin-3 mediates nuclear beta-catenin accumulation and Wnt signaling in human colon cancer cells by regulation of glycogen synthase kinase-3beta activity Cancer Res. 69 2009 1343 1349
    • (2009) Cancer Res. , vol.69 , pp. 1343-1349
    • Song, S.1    Mazurek, N.2    Liu, C.3    Sun, Y.4    Ding, Q.Q.5    Liu, K.6    Hung, M.C.7    Bresalier, R.S.8
  • 14
    • 67649795958 scopus 로고    scopus 로고
    • Galectin-3 regulates T-cell functions
    • D.K. Hsu, H.Y. Chen, and F.T. Liu Galectin-3 regulates T-cell functions Immunol. Rev. 230 2009 114 127
    • (2009) Immunol. Rev. , vol.230 , pp. 114-127
    • Hsu, D.K.1    Chen, H.Y.2    Liu, F.T.3
  • 16
    • 70350428098 scopus 로고    scopus 로고
    • The role of galectins in protein trafficking
    • D. Delacour, A. Koch, and R. Jacob The role of galectins in protein trafficking Traffic 10 2009 1405 1413
    • (2009) Traffic , vol.10 , pp. 1405-1413
    • Delacour, D.1    Koch, A.2    Jacob, R.3
  • 17
  • 19
    • 84861596300 scopus 로고    scopus 로고
    • Cell-surface galectin-3 confers resistance to TRAIL by impeding trafficking of death receptors in metastatic colon adenocarcinoma cells
    • N. Mazurek, J.C. Byrd, Y. Sun, M. Hafley, K. Ramirez, J. Burks, and R.S. Bresalier Cell-surface galectin-3 confers resistance to TRAIL by impeding trafficking of death receptors in metastatic colon adenocarcinoma cells Cell Death Differ. 2011
    • (2011) Cell Death Differ.
    • Mazurek, N.1    Byrd, J.C.2    Sun, Y.3    Hafley, M.4    Ramirez, K.5    Burks, J.6    Bresalier, R.S.7
  • 22
    • 67649831425 scopus 로고    scopus 로고
    • The regulation of inflammation by galectin-3
    • N.C. Henderson, and T. Sethi The regulation of inflammation by galectin-3 Immunol. Rev. 230 2009 160 171
    • (2009) Immunol. Rev. , vol.230 , pp. 160-171
    • Henderson, N.C.1    Sethi, T.2
  • 25
    • 0025963002 scopus 로고
    • The human leukemia cell line, THP-1: A multifacetted model for the study of monocyte-macrophage differentiation
    • J. Auwerx The human leukemia cell line, THP-1: a multifacetted model for the study of monocyte-macrophage differentiation Experientia 47 1991 22 31
    • (1991) Experientia , vol.47 , pp. 22-31
    • Auwerx, J.1
  • 26
    • 24044439159 scopus 로고    scopus 로고
    • The macrophage alphaMbeta2 integrin alphaM lectin domain mediates the phagocytosis of chilled platelets
    • E.C. Josefsson, H.H. Gebhard, T.P. Stossel, J.H. Hartwig, and K.M. Hoffmeister The macrophage alphaMbeta2 integrin alphaM lectin domain mediates the phagocytosis of chilled platelets J. Biol. Chem. 280 2005 18025 18032
    • (2005) J. Biol. Chem. , vol.280 , pp. 18025-18032
    • Josefsson, E.C.1    Gebhard, H.H.2    Stossel, T.P.3    Hartwig, J.H.4    Hoffmeister, K.M.5
  • 28
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • F. Martinon, K. Burns, and J. Tschopp The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta Mol. Cell 10 2002 417 426
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 29
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • R. Zhou, A.S. Yazdi, P. Menu, and J. Tschopp A role for mitochondria in NLRP3 inflammasome activation Nature 469 2011 221 225
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 30
    • 0037218268 scopus 로고    scopus 로고
    • THP-1 cell apoptosis in response to Mycobacterial infection
    • C.J. Riendeau, and H. Kornfeld THP-1 cell apoptosis in response to Mycobacterial infection Infect. Immun. 71 2003 254 259
    • (2003) Infect. Immun. , vol.71 , pp. 254-259
    • Riendeau, C.J.1    Kornfeld, H.2
  • 31
    • 0033543975 scopus 로고    scopus 로고
    • The receptor-mediated uptake, survival, replication, and drug sensitivity of Mycobacterium tuberculosis within the macrophage-like cell line THP-1: A comparison with human monocyte-derived macrophages
    • R.W. Stokes, and D. Doxsee The receptor-mediated uptake, survival, replication, and drug sensitivity of Mycobacterium tuberculosis within the macrophage-like cell line THP-1: a comparison with human monocyte-derived macrophages Cell. Immunol. 197 1999 1 9
    • (1999) Cell. Immunol. , vol.197 , pp. 1-9
    • Stokes, R.W.1    Doxsee, D.2
  • 34
    • 0026762988 scopus 로고
    • Interleukin 4 potently enhances murine macrophage mannose receptor activity: A marker of alternative immunologic macrophage activation
    • M. Stein, S. Keshav, N. Harris, and S. Gordon Interleukin 4 potently enhances murine macrophage mannose receptor activity: a marker of alternative immunologic macrophage activation J. Exp. Med. 176 1992 287 292
    • (1992) J. Exp. Med. , vol.176 , pp. 287-292
    • Stein, M.1    Keshav, S.2    Harris, N.3    Gordon, S.4
  • 37
    • 33745698459 scopus 로고    scopus 로고
    • Enhancement of bound-state residual dipolar couplings: Conformational analysis of lactose bound to Galectin-3
    • T. Zhuang, H. Leffler, and J.H. Prestegard Enhancement of bound-state residual dipolar couplings: conformational analysis of lactose bound to Galectin-3 Protein Sci. 15 2006 1780 1790
    • (2006) Protein Sci. , vol.15 , pp. 1780-1790
    • Zhuang, T.1    Leffler, H.2    Prestegard, J.H.3
  • 38
    • 35848939621 scopus 로고    scopus 로고
    • Lipopolysaccharide challenge of humans as a model for chronic obstructive lung disease exacerbations
    • S.A. Kharitonov, and U. Sjobring Lipopolysaccharide challenge of humans as a model for chronic obstructive lung disease exacerbations Contrib. Microbiol. 14 2007 83 100
    • (2007) Contrib. Microbiol. , vol.14 , pp. 83-100
    • Kharitonov, S.A.1    Sjobring, U.2
  • 39
    • 0034984262 scopus 로고    scopus 로고
    • Innate immunity and inflammation: A transcriptional paradigm
    • J. Hawiger Innate immunity and inflammation: a transcriptional paradigm Immunol. Res. 23 2001 99 109
    • (2001) Immunol. Res. , vol.23 , pp. 99-109
    • Hawiger, J.1
  • 41
    • 34548736515 scopus 로고    scopus 로고
    • Intracellular sorting of galectin-8 based on carbohydrate fine specificity
    • S. Carlsson, M.C. Carlsson, and H. Leffler Intracellular sorting of galectin-8 based on carbohydrate fine specificity Glycobiology 17 2007 906 912
    • (2007) Glycobiology , vol.17 , pp. 906-912
    • Carlsson, S.1    Carlsson, M.C.2    Leffler, H.3
  • 42
    • 77955335001 scopus 로고    scopus 로고
    • 1H-1,2,3-triazol-1-yl thiodigalactoside derivatives as high affinity galectin-3 inhibitors
    • B.A. Salameh, I. Cumpstey, A. Sundin, H. Leffler, and U.J. Nilsson 1H-1,2,3-triazol-1-yl thiodigalactoside derivatives as high affinity galectin-3 inhibitors Bioorg. Med. Chem. 18 2010 5367 5378
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 5367-5378
    • Salameh, B.A.1    Cumpstey, I.2    Sundin, A.3    Leffler, H.4    Nilsson, U.J.5
  • 43
    • 39049094267 scopus 로고    scopus 로고
    • Human IgG/Fc gamma R interactions are modulated by streptococcal IgG glycan hydrolysis
    • M. Allhorn, A.I. Olin, F. Nimmerjahn, and M. Collin Human IgG/Fc gamma R interactions are modulated by streptococcal IgG glycan hydrolysis PLoS One 3 2008 e1413
    • (2008) PLoS One , vol.3 , pp. 1413
    • Allhorn, M.1    Olin, A.I.2    Nimmerjahn, F.3    Collin, M.4
  • 44
    • 33645102970 scopus 로고    scopus 로고
    • Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells
    • S.K. Patnaik, B. Potvin, S. Carlsson, D. Sturm, H. Leffler, and P. Stanley Complex N-glycans are the major ligands for galectin-1, -3, and -8 on Chinese hamster ovary cells Glycobiology 16 2006 305 317
    • (2006) Glycobiology , vol.16 , pp. 305-317
    • Patnaik, S.K.1    Potvin, B.2    Carlsson, S.3    Sturm, D.4    Leffler, H.5    Stanley, P.6
  • 45
    • 33646106334 scopus 로고    scopus 로고
    • Galectin-3 in macrophage-like cells exposed to immunomodulatory drugs
    • S. Dabelic, S. Supraha, and J. Dumic Galectin-3 in macrophage-like cells exposed to immunomodulatory drugs Biochim. Biophys. Acta 1760 2006 701 709
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 701-709
    • Dabelic, S.1    Supraha, S.2    Dumic, J.3
  • 46
    • 0037265240 scopus 로고    scopus 로고
    • Alternative activation of macrophages
    • S. Gordon Alternative activation of macrophages Nat. Rev. Immunol. 3 2003 23 35
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 23-35
    • Gordon, S.1
  • 47
    • 84861624905 scopus 로고    scopus 로고
    • Galectin-1 and galectin-3 expression profiles in classically and alternatively activated human macrophages
    • R. Novak, S. Dabelic, and J. Dumic Galectin-1 and galectin-3 expression profiles in classically and alternatively activated human macrophages Biochim. Biophys. Acta 2011
    • (2011) Biochim. Biophys. Acta
    • Novak, R.1    Dabelic, S.2    Dumic, J.3
  • 48
    • 0028047113 scopus 로고
    • Mac-2: A versatile galactose-binding protein of mammalian tissues
    • R.C. Hughes Mac-2: a versatile galactose-binding protein of mammalian tissues Glycobiology 4 1994 5 12
    • (1994) Glycobiology , vol.4 , pp. 5-12
    • Hughes, R.C.1
  • 49
    • 0028009934 scopus 로고
    • Control of Mac-2 surface expression on murine macrophage cell lines
    • S. Sato, and R.C. Hughes Control of Mac-2 surface expression on murine macrophage cell lines Eur. J. Immunol. 24 1994 216 221
    • (1994) Eur. J. Immunol. , vol.24 , pp. 216-221
    • Sato, S.1    Hughes, R.C.2
  • 50
    • 44949125365 scopus 로고    scopus 로고
    • Distinct effects on splicing of two monoclonal antibodies directed against the amino-terminal domain of galectin-3
    • R.M. Gray, M.J. Davis, K.M. Ruby, P.G. Voss, R.J. Patterson, and J.L. Wang Distinct effects on splicing of two monoclonal antibodies directed against the amino-terminal domain of galectin-3 Arch. Biochem. Biophys. 475 2008 100 108
    • (2008) Arch. Biochem. Biophys. , vol.475 , pp. 100-108
    • Gray, R.M.1    Davis, M.J.2    Ruby, K.M.3    Voss, P.G.4    Patterson, R.J.5    Wang, J.L.6
  • 51
    • 69949159693 scopus 로고    scopus 로고
    • Sugar-free antibodies - The bacterial solution to autoimmunity?
    • M. Allhorn, and M. Collin Sugar-free antibodies - the bacterial solution to autoimmunity? Ann. N. Y. Acad. Sci. 1173 2009 664 669
    • (2009) Ann. N. Y. Acad. Sci. , vol.1173 , pp. 664-669
    • Allhorn, M.1    Collin, M.2
  • 52
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • L.H. Wang, K.G. Rothberg, and R.G. Anderson Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation J. Cell Biol. 123 1993 1107 1117
    • (1993) J. Cell Biol. , vol.123 , pp. 1107-1117
    • Wang, L.H.1    Rothberg, K.G.2    Anderson, R.G.3
  • 53
    • 0037684840 scopus 로고    scopus 로고
    • Caveolae/raft-dependent endocytosis
    • I.R. Nabi, and P.U. Le Caveolae/raft-dependent endocytosis J. Cell Biol. 161 2003 673 677
    • (2003) J. Cell Biol. , vol.161 , pp. 673-677
    • Nabi, I.R.1    Le, P.U.2
  • 54
    • 0021219683 scopus 로고
    • Characterization of potent Na+/H+ exchange inhibitors from the amiloride series in A431 cells
    • Y. Zhuang, E.J. Cragoe Jr., T. Shaikewitz, L. Glaser, and D. Cassel Characterization of potent Na+/H+ exchange inhibitors from the amiloride series in A431 cells Biochemistry 23 1984 4481 4488
    • (1984) Biochemistry , vol.23 , pp. 4481-4488
    • Zhuang, Y.1    Cragoe, Jr.E.J.2    Shaikewitz, T.3    Glaser, L.4    Cassel, D.5
  • 55
    • 29144443587 scopus 로고    scopus 로고
    • Molecular analysis of expression and function of hFcgammaRIIbl and b2 isoforms in myeloid cells
    • T. Joshi, L.P. Ganesan, X. Cao, and S. Tridandapani Molecular analysis of expression and function of hFcgammaRIIbl and b2 isoforms in myeloid cells Mol. Immunol. 43 2006 839 850
    • (2006) Mol. Immunol. , vol.43 , pp. 839-850
    • Joshi, T.1    Ganesan, L.P.2    Cao, X.3    Tridandapani, S.4
  • 56
    • 0027418205 scopus 로고
    • Measurement of co-localization of objects in dual-colour confocal images
    • V.a.A. Manders Measurement of co-localization of objects in dual-colour confocal images J. Microsc. 169 1993 375 382
    • (1993) J. Microsc. , vol.169 , pp. 375-382
    • Manders A. V, A.1
  • 57
    • 0026770786 scopus 로고
    • Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin
    • D.K. Hsu, R.I. Zuberi, and F.T. Liu Biochemical and biophysical characterization of human recombinant IgE-binding protein, an S-type animal lectin J. Biol. Chem. 267 1992 14167 14174
    • (1992) J. Biol. Chem. , vol.267 , pp. 14167-14174
    • Hsu, D.K.1    Zuberi, R.I.2    Liu, F.T.3
  • 58
    • 0027492711 scopus 로고
    • L-29, an endogenous lectin, binds to glycoconjugate ligands with positive cooperativity
    • S.M. Massa, D.N. Cooper, H. Leffler, and S.H. Barondes L-29, an endogenous lectin, binds to glycoconjugate ligands with positive cooperativity Biochemistry 32 1993 260 267
    • (1993) Biochemistry , vol.32 , pp. 260-267
    • Massa, S.M.1    Cooper, D.N.2    Leffler, H.3    Barondes, S.H.4
  • 59
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • N. Ahmad, H.J. Gabius, S. Andre, H. Kaltner, S. Sabesan, R. Roy, B. Liu, F. Macaluso, and C.F. Brewer Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes J. Biol. Chem. 279 2004 10841 10847
    • (2004) J. Biol. Chem. , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.J.2    Andre, S.3    Kaltner, H.4    Sabesan, S.5    Roy, R.6    Liu, B.7    MacAluso, F.8    Brewer, C.F.9
  • 60
    • 0035901521 scopus 로고    scopus 로고
    • NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: Evidence for interactions between the N- and C-terminal domains
    • B. Birdsall, J. Feeney, I.D. Burdett, S. Bawumia, E.A. Barboni, and R.C. Hughes NMR solution studies of hamster galectin-3 and electron microscopic visualization of surface-adsorbed complexes: evidence for interactions between the N- and C-terminal domains Biochemistry 40 2001 4859 4866
    • (2001) Biochemistry , vol.40 , pp. 4859-4866
    • Birdsall, B.1    Feeney, J.2    Burdett, I.D.3    Bawumia, S.4    Barboni, E.A.5    Hughes, R.C.6
  • 61
    • 0000594001 scopus 로고    scopus 로고
    • Role of the carboxyl-terminal lectin domain in self-association of galectin-3
    • R.Y. Yang, P.N. Hill, D.K. Hsu, and F.T. Liu Role of the carboxyl-terminal lectin domain in self-association of galectin-3 Biochemistry 37 1998 4086 4092
    • (1998) Biochemistry , vol.37 , pp. 4086-4092
    • Yang, R.Y.1    Hill, P.N.2    Hsu, D.K.3    Liu, F.T.4
  • 62
    • 50249138175 scopus 로고    scopus 로고
    • Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis
    • R. Fajka-Boja, A. Blasko, F. Kovacs-Solyom, G.J. Szebeni, G.K. Toth, and E. Monostori Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis Cell. Mol. Life Sci. 65 2008 2586 2593
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2586-2593
    • Fajka-Boja, R.1    Blasko, A.2    Kovacs-Solyom, F.3    Szebeni, G.J.4    Toth, G.K.5    Monostori, E.6
  • 64
    • 33749143645 scopus 로고    scopus 로고
    • Specific recognition of Candida albicans by macrophages requires galectin-3 to discriminate Saccharomyces cerevisiae and needs association with TLR2 for signaling
    • T. Jouault, M. El Abed-El Behi, M. Martinez-Esparza, L. Breuilh, P.A. Trinel, M. Chamaillard, F. Trottein, and D. Poulain Specific recognition of Candida albicans by macrophages requires galectin-3 to discriminate Saccharomyces cerevisiae and needs association with TLR2 for signaling J. Immunol. 177 2006 4679 4687
    • (2006) J. Immunol. , vol.177 , pp. 4679-4687
    • Jouault, T.1    El Abed-El Behi, M.2    Martinez-Esparza, M.3    Breuilh, L.4    Trinel, P.A.5    Chamaillard, M.6    Trottein, F.7    Poulain, D.8
  • 65
    • 75749101401 scopus 로고    scopus 로고
    • Galectins: Regulators of acute and chronic inflammation
    • F.T. Liu, and G.A. Rabinovich Galectins: regulators of acute and chronic inflammation Ann. N. Y. Acad. Sci. 1183 2010 158 182
    • (2010) Ann. N. Y. Acad. Sci. , vol.1183 , pp. 158-182
    • Liu, F.T.1    Rabinovich, G.A.2


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