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Volumn 186, Issue , 2002, Pages 47-56

A novel adhesion pathway that regulates dendritic cell trafficking and T cell interactions

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; INTERCELLULAR ADHESION MOLECULE 2; INTERCELLULAR ADHESION MOLECULE 3; LECTIN; LECTIN RECEPTOR; LYMPHOCYTE ANTIGEN RECEPTOR; MANNOSE; CD209 ANTIGEN; CELL ADHESION MOLECULE; CELL SURFACE RECEPTOR; DC-SPECIFIC ICAM-3 GRABBING NONINTEGRIN;

EID: 0036696154     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2002.18605.x     Document Type: Review
Times cited : (71)

References (52)
  • 1
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Bancherean J, Steinman RM. Dendritic cells and the control of immunity. Nature 1998;392:245-252.
    • (1998) Nature , vol.392 , pp. 245-252
    • Bancherean, J.1    Steinman, R.M.2
  • 2
    • 0033557170 scopus 로고    scopus 로고
    • Mobilizing dendritic cells for tolerance, priming, and chronic inflammation
    • Sallusto F, Lanzavecchia A. Mobilizing dendritic cells for tolerance, priming, and chronic inflammation. J Exp Med 1999;189:611-614.
    • (1999) J Exp Med , vol.189 , pp. 611-614
    • Sallusto, F.1    Lanzavecchia, A.2
  • 3
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek TBH, et al. Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 2000;100:575-585.
    • (2000) Cell , vol.100 , pp. 575-585
    • Geijtenbeek, T.B.H.1
  • 4
    • 0026756506 scopus 로고
    • Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120
    • Curtis BM, Scharnowske S, Watson AJ. Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120. Proc Natl Acad Sci USA 1992;89:8356-8360.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8356-8360
    • Curtis, B.M.1    Scharnowske, S.2    Watson, A.J.3
  • 5
    • 0034304945 scopus 로고    scopus 로고
    • DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking
    • Geijtenbeek TBH, et al. DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking. Nature Immunol 2000;1:353-357.
    • (2000) Nature Immunol , vol.1 , pp. 353-357
    • Geijtenbeek, T.B.H.1
  • 7
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk Y, Figdor CG. Avidity regulation of integrins: the driving force in leukocyte adhesion. Curr Opin Cell Biol 2000;12:542-547.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 542-547
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 8
    • 0035800757 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands
    • Mitchell DA, Fadden AJ, Drickamer K. A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands. J Biol Chem 2001;276:28939-28945.
    • (2001) J Biol Chem , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 9
    • 0035058780 scopus 로고    scopus 로고
    • Structural study of N-linked oligosaccharides of human intercellular adhesion molecule-3 (CD50)
    • Funatsu O, Sato T, Kotovuori P, Gahmberg CG, Ikekita M, Furukawa K. Structural study of N-linked oligosaccharides of human intercellular adhesion molecule-3 (CD50). Eur J Biochem 2001;268:1020-1029.
    • (2001) Eur J Biochem , vol.268 , pp. 1020-1029
    • Funatsu, O.1    Sato, T.2    Kotovuori, P.3    Gahmberg, C.G.4    Ikekita, M.5    Furukawa, K.6
  • 10
    • 0037192786 scopus 로고    scopus 로고
    • Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for ICAM-3 and HIV-1
    • Geijtenbeek TBH, et al. Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for ICAM-3 and HIV-1. J Biol Chem; 2002;277:11314-11320.
    • (2002) J Biol Chem , vol.277 , pp. 11314-11320
    • Geijtenbeek, T.B.H.1
  • 11
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond MS, Springer TA. The dynamic regulation of integrin adhesiveness. Curr Biol. 1994;4:506-517.
    • (1994) Curr Biol , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 13
    • 0035663209 scopus 로고    scopus 로고
    • Placental expression of DC-SIGN may mediate intrauterine vertical transmission of HIV
    • Soilleux EJ, et al. Placental expression of DC-SIGN may mediate intrauterine vertical transmission of HIV. J Pathol 2001;195:586-592.
    • (2001) J Pathol , vol.195 , pp. 586-592
    • Soilleux, E.J.1
  • 14
  • 15
    • 0035194354 scopus 로고    scopus 로고
    • cis expression of DC-SIGN allows for more efficient entry of human and simian immunodeficiency viruses via CD4 and a coreceptor
    • Lee B, et al. cis Expression of DC-SIGN allows for more efficient entry of human and simian immunodeficiency viruses via CD4 and a coreceptor. J Virol 2001;75:12028-12038.
    • (2001) J Virol , vol.75 , pp. 12028-12038
    • Lee, B.1
  • 16
    • 0036521487 scopus 로고    scopus 로고
    • Constitutive and induced expression of DC-SIGN on dendritic cell and macrophage subpopulations in situ and in vitro
    • Soilleux EJ, et al. Constitutive and induced expression of DC-SIGN on dendritic cell and macrophage subpopulations in situ and in vitro. J Leukoc Biol 2002;71:445-457.
    • (2002) J Leukoc Biol , vol.71 , pp. 445-457
    • Soilleux, E.J.1
  • 17
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer TA. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 1994;76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 18
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their ligands
    • Vestweber D, Blanks JE. Mechanisms that regulate the function of the selectins and their ligands. Physiol Rev 1999;79:181-213.
    • (1999) Physiol Rev , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.E.2
  • 19
    • 0034599815 scopus 로고    scopus 로고
    • The cysteine-rich domain of the macrophage mannose receptor is a multispecific lectin that recognizes chondroitin sulfates A and B and sulfated oligosaccharides of blood group Lewis (a) and Lewis (x) types in addition to the sulfated N-glycans of lutropin
    • Leteux C, et al. The cysteine-rich domain of the macrophage mannose receptor is a multispecific lectin that recognizes chondroitin sulfates A and B and sulfated oligosaccharides of blood group Lewis (a) and Lewis (x) types in addition to the sulfated N-glycans of lutropin. J Exp Med 2000;191:1117-1126.
    • (2000) J Exp Med , vol.191 , pp. 1117-1126
    • Leteux, C.1
  • 20
    • 0035886820 scopus 로고    scopus 로고
    • Mannose receptor is a novel ligand for 1-selectin and mediates lymphocyte binding to lymphatic endothelium
    • Irjala H, Johansson EL, Grenman R, Alanen K, Salmi M, Jalkanen S. Mannose receptor is a novel ligand for 1-selectin and mediates lymphocyte binding to lymphatic endothelium. J Exp Med 2001;194:1033-1042.
    • (2001) J Exp Med , vol.194 , pp. 1033-1042
    • Irjala, H.1    Johansson, E.L.2    Grenman, R.3    Alanen, K.4    Salmi, M.5    Jalkanen, S.6
  • 21
    • 17944382137 scopus 로고    scopus 로고
    • Sulfation of 1-selectin ligands by an HEV-restricted sulfotransferase regulates lymphocyte homing to lymph nodes
    • Hemmerich S, et al. Sulfation of 1-selectin ligands by an HEV-restricted sulfotransferase regulates lymphocyte homing to lymph nodes. Immunity 2001;15:237-247.
    • (2001) Immunity , vol.15 , pp. 237-247
    • Hemmerich, S.1
  • 22
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation dusters in T cells
    • Monks CR, Freiberg BA, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation dusters in T cells. Nature 1998;395:82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 23
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • Grakoui A, et al. The immunological synapse: a molecular machine controlling T cell activation. Science 1999;285:221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 24
    • 0034644505 scopus 로고    scopus 로고
    • Signaling takes shape in the immune system
    • Dustin ML, Chart AC. Signaling takes shape in the immune system. Cell 2000;103:283-294.
    • (2000) Cell , vol.103 , pp. 283-294
    • Dustin, M.L.1    Chart, A.C.2
  • 25
    • 0026693787 scopus 로고
    • Isolation, characterization, and expression of mouse ICAM-2 complementary and genomic DNA
    • Xu H, Tong IL, De Fougerolles AR, Springer TA. Isolation, characterization, and expression of mouse ICAM-2 complementary and genomic DNA. J Immunol 1992;149:2650-2655.
    • (1992) J Immunol , vol.149 , pp. 2650-2655
    • Xu, H.1    Tong, I.L.2    De Fougerolles, A.R.3    Springer, T.A.4
  • 27
    • 0029126797 scopus 로고
    • Intercellular adhesion molecule-3 is the predominant co-stimulatory ligand for leukocyte function antigen-1 on human blood dendritic cells
    • Starling GC, et al. Intercellular adhesion molecule-3 is the predominant co-stimulatory ligand for leukocyte function antigen-1 on human blood dendritic cells. Eur J Immunol 1995;25:2528-2532.
    • (1995) Eur J Immunol , vol.25 , pp. 2528-2532
    • Starling, G.C.1
  • 29
    • 0036172558 scopus 로고    scopus 로고
    • Role of ICAM-3 in the initial interaction of T lymphocytes and APCs
    • Montoya MC, et al. Role of ICAM-3 in the initial interaction of T lymphocytes and APCs. Nat Immunol 2002;3:159-168.
    • (2002) Nat Immunol , vol.3 , pp. 159-168
    • Montoya, M.C.1
  • 30
    • 0034733654 scopus 로고    scopus 로고
    • Identification of a novel, dendritic cell-associated molecule, dectin-1, by subtractive cDNA cloning
    • Ariizumi K, et al. Identification of a novel, dendritic cell-associated molecule, dectin-1, by subtractive cDNA cloning. J Biol Chem 2000;275:20157-20167.
    • (2000) J Biol Chem , vol.275 , pp. 20157-20167
    • Ariizumi, K.1
  • 31
    • 0035941226 scopus 로고    scopus 로고
    • Characterization of the human beta-glucan receptor and its alternatively spliced isoforms
    • Willment JA, Gordon S, Brown GD. Characterization of the human beta-glucan receptor and its alternatively spliced isoforms. J Biol Chem 2001;276:43818-43823.
    • (2001) J Biol Chem , vol.276 , pp. 43818-43823
    • Willment, J.A.1    Gordon, S.2    Brown, G.D.3
  • 32
    • 0029148878 scopus 로고
    • Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: Downregulation by cytokines and bacterial products
    • Sallusto F, Cella M, Danieli C, Lanzavecchia A. Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: downregulation by cytokines and bacterial products. J Exp Med 1995;182:389-400.
    • (1995) J Exp Med , vol.182 , pp. 389-400
    • Sallusto, F.1    Cella, M.2    Danieli, C.3    Lanzavecchia, A.4
  • 33
    • 0033739798 scopus 로고    scopus 로고
    • Expression of multilectin receptors and comparative FITC-dextran uptake by human dendritic cells
    • Kato M, Neil TK, Fearnley DB, McLellan AD, Vuckovic S, Hart DN. Expression of multilectin receptors and comparative FITC-dextran uptake by human dendritic cells. Int Immunol 2000;12:1511-1519.
    • (2000) Int Immunol , vol.12 , pp. 1511-1519
    • Kato, M.1    Neil, T.K.2    Fearnley, D.B.3    McLellan, A.D.4    Vuckovic, S.5    Hart, D.N.6
  • 34
    • 0035905321 scopus 로고    scopus 로고
    • BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction
    • Dzionek A, et al. BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction. J Exp Med 2001;194:1823-1834.
    • (2001) J Exp Med , vol.194 , pp. 1823-1834
    • Dzionek, A.1
  • 35
    • 0035889925 scopus 로고    scopus 로고
    • Immature human dendritic cells express asialoglycoprotein receptor isoforms for efficient receptor-mediated endocytosis
    • Valladeau J, et al. Immature human dendritic cells express asialoglycoprotein receptor isoforms for efficient receptor-mediated endocytosis. J Immunol 2001;167:5767-5774.
    • (2001) J Immunol , vol.167 , pp. 5767-5774
    • Valladeau, J.1
  • 36
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg H, Mitchell DA, Drickamer K, Weis WI. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 2001;294:2163-2166.
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 37
    • 0036481121 scopus 로고    scopus 로고
    • C-type lectin receptors on dendritic cells and Langerhans cells
    • Figdor CG, van Kooyk Y, Adema GJ. C-type lectin receptors on dendritic cells and Langerhans cells. Nature Rev Immunol 2002;2:77-84.
    • (2002) Nature Rev Immunol , vol.2 , pp. 77-84
    • Figdor, C.G.1    Van Kooyk, Y.2    Adema, G.J.3
  • 38
    • 0028882008 scopus 로고
    • Increasing diversity of animal lectin structures
    • Drickamer K. Increasing diversity of animal lectin structures. Curr Opin Struct Biol 1995;5:612-616.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 612-616
    • Drickamer, K.1
  • 39
    • 0026561385 scopus 로고
    • The mannose receptor and other macrophage lectins
    • Stahl PD. The mannose receptor and other macrophage lectins. Curr Opin Immunol 1992;4:49-52.
    • (1992) Curr Opin Immunol , vol.4 , pp. 49-52
    • Stahl, P.D.1
  • 40
    • 0025608606 scopus 로고
    • Molecular characterization of the human macrophage mannose receptor: Demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells
    • Ezekowitz PA, Sastry K, Bailly P, Warner A. Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells. J Exp Med 1990;172:1785-1794.
    • (1990) J Exp Med , vol.172 , pp. 1785-1794
    • Ezekowitz, P.A.1    Sastry, K.2    Bailly, P.3    Warner, A.4
  • 41
    • 0030772131 scopus 로고    scopus 로고
    • The mannose receptor functions as a high capacity and broad specificity antigen receptor in human dendritic cells
    • Engering AJ, et al. The mannose receptor functions as a high capacity and broad specificity antigen receptor in human dendritic cells. Eur J Immunol 1997;27:2417-2425.
    • (1997) Eur J Immunol , vol.27 , pp. 2417-2425
    • Engering, A.J.1
  • 42
    • 0030824448 scopus 로고    scopus 로고
    • Mannose receptor-mediated uptake of antigens strongly enhances HLA class II-restricted antigen presentation by cultured dendritic cells
    • Tan MC, et al. Mannose receptor-mediated uptake of antigens strongly enhances HLA class II-restricted antigen presentation by cultured dendritic cells. Eur J Immunol 1997;27:2426-2435.
    • (1997) Eur J Immunol , vol.27 , pp. 2426-2435
    • Tan, M.C.1
  • 43
    • 0036499125 scopus 로고    scopus 로고
    • The dendritic cell-specific adhesionreceptor DC-SIGN internalizes antigen for presentation to T cells
    • Engering A, et al. The dendritic cell-specific adhesionreceptor DC-SIGN internalizes antigen for presentation to T cells. J Immunol; 2002;168:2118-2126.
    • (2002) J Immunol , vol.168 , pp. 2118-2126
    • Engering, A.1
  • 44
    • 0034503091 scopus 로고    scopus 로고
    • The ITAM-bearing transmembrane adaptor DAP12 in lymphoid and myeloid cell function
    • Lanier LL, Bakker AB. The ITAM-bearing transmembrane adaptor DAP12 in lymphoid and myeloid cell function. Immunol Today 2000;21:611-614.
    • (2000) Immunol Today , vol.21 , pp. 611-614
    • Lanier, L.L.1    Bakker, A.B.2
  • 45
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HW-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek TBH, et al. DC-SIGN, a dendritic cell-specific HW-1-binding protein that enhances trans-infection of T cells. Cell 2000;100:587-597.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.H.1
  • 46
    • 0036172314 scopus 로고    scopus 로고
    • DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection
    • Kwon DS, Gregorio G, Bitton N, Hendrickson WA, Littman DR. DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection. Immunity 2002;16:135-144.
    • (2002) Immunity , vol.16 , pp. 135-144
    • Kwon, D.S.1    Gregorio, G.2    Bitton, N.3    Hendrickson, W.A.4    Littman, D.R.5
  • 47
    • 0035919709 scopus 로고    scopus 로고
    • Nef is required for efficient HIV-1 replication in cocultures of dendritic cells and lymphocytes
    • Petit C, Buseyne F, Boccaccio C, Abastado JP, Heard JM, Schwartz O. Nef is required for efficient HIV-1 replication in cocultures of dendritic cells and lymphocytes. Virology 2001;286:225-236.
    • (2001) Virology , vol.286 , pp. 225-236
    • Petit, C.1    Buseyne, F.2    Boccaccio, C.3    Abastado, J.P.4    Heard, J.M.5    Schwartz, O.6
  • 48
    • 0033515427 scopus 로고    scopus 로고
    • Nef-induced CD4 degradation. A diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes
    • Piguet V, et al. Nef-induced CD4 degradation. a diacidic-based motif in Nef functions as a lysosomal targeting signal through the binding of beta-COP in endosomes. Cell 1999;97:63-73.
    • (1999) Cell , vol.97 , pp. 63-73
    • Piguet, V.1
  • 49
    • 0036169006 scopus 로고    scopus 로고
    • HIV-1 nef induced upregulation of DC-SIGN in dendritic cells promotes lymphocyte clustering and viral spread
    • Sol-Foulon N, et al. HIV-1 nef induced upregulation of DC-SIGN in dendritic cells promotes lymphocyte clustering and viral spread. Immunity 2002;16:145-155.
    • (2002) Immunity , vol.16 , pp. 145-155
    • Sol-Foulon, N.1
  • 50
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis WI, Taylor ME, Drickamer K. The C-type lectin superfamily in the immune system. Immunol Rev 1998;163:19-34.
    • (1998) Immunol Rev , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 51
    • 0034772132 scopus 로고    scopus 로고
    • Five mouse homologues of the human dendritic cell C-type lectin, DC-SIGN
    • Park CG, et al. Five mouse homologues of the human dendritic cell C-type lectin, DC-SIGN. Int Immunol 2001;11:1283-1290.
    • (2001) Int Immunol , vol.11 , pp. 1283-1290
    • Park, C.G.1
  • 52
    • 0034773020 scopus 로고    scopus 로고
    • Molecular cloning of a C-type lectin superfamily protein differentially expressed by CD8alpha (-) splenic dendritic cells
    • Caminschi I, et al. Molecular cloning of a C-type lectin superfamily protein differentially expressed by CD8alpha (-) splenic dendritic cells. Mol Immunol 2001;38:365-373.
    • (2001) Mol Immunol , vol.38 , pp. 365-373
    • Caminschi, I.1


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