메뉴 건너뛰기




Volumn 185, Issue 7, 2010, Pages 3847-3856

Cell surface heparan sulfate proteoglycans influence MHC class II-restricted antigen presentation

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PROTEOHEPARAN SULFATE; TRANSACTIVATOR PROTEIN; HLA ANTIGEN CLASS 2;

EID: 77958138601     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0902724     Document Type: Article
Times cited : (13)

References (44)
  • 1
    • 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., M. Cella, C. Danieli, and A. Lanzavecchia. 1995. 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. 182:389-400.
    • (1995) J. Exp. Med. , vol.182 , pp. 389-400
    • Sallusto, F.1    Cella, M.2    Danieli, C.3    Lanzavecchia, A.4
  • 2
    • 0030175501 scopus 로고    scopus 로고
    • Mechanisms of antigen uptake for presentation
    • Lanzavecchia, A. 1996. Mechanisms of antigen uptake for presentation. Curr. Opin. Immunol. 8:348-354.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 348-354
    • Lanzavecchia, A.1
  • 3
    • 0030937833 scopus 로고    scopus 로고
    • Capture and processing of exogenous antigens for presentation on MHC molecules
    • Watts, C. 1997. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 15:821-850.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 821-850
    • Watts, C.1
  • 4
    • 0035140119 scopus 로고    scopus 로고
    • The cell biology of antigen presentation in dendritic cells
    • Théry, C., and S. Amigorena. 2001. The cell biology of antigen presentation in dendritic cells. Curr. Opin. Immunol. 13:45-51.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 45-51
    • Théry, C.1    Amigorena, S.2
  • 6
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha
    • Sallusto, F., and A. Lanzavecchia. 1994. Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha. J. Exp. Med. 179:1109-1118.
    • (1994) J. Exp. Med. , vol.179 , pp. 1109-1118
    • Sallusto, F.1    Lanzavecchia, A.2
  • 7
    • 0034730728 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycans: Selective regulators of ligand-receptor encounters
    • Park, P. W., O. Reizes, and M. Bernfield. 2000. Cell surface heparan sulfate proteoglycans: selective regulators of ligand-receptor encounters. J. Biol. Chem. 275:29923-29926.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29923-29926
    • Park, P.W.1    Reizes, O.2    Bernfield, M.3
  • 8
    • 0032788960 scopus 로고    scopus 로고
    • Glycosaminoglycan-binding microbial proteins in tissue adhesion and invasion: Key events in microbial pathogenicity
    • Wadström, T., and A. Ljungh. 1999. Glycosaminoglycan-binding microbial proteins in tissue adhesion and invasion: key events in microbial pathogenicity. J. Med. Microbiol. 48:223-233.
    • (1999) J. Med. Microbiol. , vol.48 , pp. 223-233
    • Wadström, T.1    Ljungh, A.2
  • 9
    • 0036273932 scopus 로고    scopus 로고
    • Enhanced bacterial virulence through exploitation of host glycosaminoglycans
    • Menozzi, F. D., K. Pethe, P. Bifani, F. Soncin, M. J. Brennan, and C. Locht. 2002. Enhanced bacterial virulence through exploitation of host glycosaminoglycans. Mol. Microbiol. 43:1379-1386.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1379-1386
    • Menozzi, F.D.1    Pethe, K.2    Bifani, P.3    Soncin, F.4    Brennan, M.J.5    Locht, C.6
  • 11
    • 0028914092 scopus 로고
    • Mediation of human immunodeficiency virus type 1 binding by interaction of cell surface heparan sulfate proteoglycans with the V3 region of envelope gp120-gp41
    • Roderiquez, G., T. Oravecz, M. Yanagishita, D. C. Bou-Habib, H. Mostowski, and M. A. Norcross. 1995. Mediation of human immunodeficiency virus type 1 binding by interaction of cell surface heparan sulfate proteoglycans with the V3 region of envelope gp120-gp41. J. Virol. 69:2233-2239.
    • (1995) J. Virol. , vol.69 , pp. 2233-2239
    • Roderiquez, G.1    Oravecz, T.2    Yanagishita, M.3    Bou-Habib, D.C.4    Mostowski, H.5    Norcross, M.A.6
  • 12
    • 0027315907 scopus 로고
    • Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate
    • Compton, T., D. M. Nowlin, and N. R. Cooper. 1993. Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate. Virology 193:834-841.
    • (1993) Virology , vol.193 , pp. 834-841
    • Compton, T.1    Nowlin, D.M.2    Cooper, N.R.3
  • 13
    • 0026525977 scopus 로고
    • Heparin enhances the interaction of infective Leishmania donovani promastigotes with mouse peritoneal macrophages. A fluorescence flow cytometric analysis
    • Butcher, B. A., L. A. Sklar, L. C. Seamer, and R. H. Glew. 1992. Heparin enhances the interaction of infective Leishmania donovani promastigotes with mouse peritoneal macrophages. A fluorescence flow cytometric analysis. J. Immunol. 148:2879-2886.
    • (1992) J. Immunol. , vol.148 , pp. 2879-2886
    • Butcher, B.A.1    Sklar, L.A.2    Seamer, L.C.3    Glew, R.H.4
  • 14
    • 0027360382 scopus 로고
    • A heparin-binding activity on Leishmania amastigotes which mediates adhesion to cellular proteoglycans
    • Love, D. C., J. D. Esko, and D. M. Mosser. 1993. A heparin-binding activity on Leishmania amastigotes which mediates adhesion to cellular proteoglycans. J. Cell Biol. 123:759-766.
    • (1993) J. Cell. Biol. , vol.123 , pp. 759-766
    • Love, D.C.1    Esko, J.D.2    Mosser, D.M.3
  • 15
    • 0028859082 scopus 로고
    • Basic fibroblast growth factor (FGF-2) internalization through the heparan sulfate proteoglycansmediated pathway: An ultrastructural approach
    • Gleizes, P. E., J. Noaillac-Depeyre, F. Amalric, and N. Gas. 1995. Basic fibroblast growth factor (FGF-2) internalization through the heparan sulfate proteoglycansmediated pathway: an ultrastructural approach. Eur. J. Cell Biol. 66:47-59.
    • (1995) Eur. J. Cell. Biol. , vol.66 , pp. 47-59
    • Gleizes, P.E.1    Noaillac-Depeyre, J.2    Amalric, F.3    Gas, N.4
  • 16
    • 0029862822 scopus 로고    scopus 로고
    • Basic fibroblast growth factor (FGF-2) is addressed to caveolae after binding to the plasma membrane of BHK cells
    • Gleizes, P. E., J. Noaillac-Depeyre, M. A. Dupont, and N. Gas. 1996. Basic fibroblast growth factor (FGF-2) is addressed to caveolae after binding to the plasma membrane of BHK cells. Eur. J. Cell Biol. 71:144-153.
    • (1996) Eur. J. Cell. Biol. , vol.71 , pp. 144-153
    • Gleizes, P.E.1    Noaillac-Depeyre, J.2    Dupont, M.A.3    Gas, N.4
  • 18
    • 0030660196 scopus 로고    scopus 로고
    • Syndecans: Multifunctional cell-surface co-receptors
    • Carey, D. J. 1997. Syndecans: multifunctional cell-surface co-receptors. Biochem. J. 327:1-16.
    • (1997) Biochem. J. , vol.327 , pp. 1-16
    • Carey, D.J.1
  • 19
    • 0025601773 scopus 로고
    • Immunization with a peptide having both T cell and conformationally restricted B cell epitopes elicits neutralizing antisera against a snake neurotoxin
    • Léonetti, M., L. Pillet, B. Maillère, H. Lamthanh, P. Frachon, J. Couderc, and A. Ménez. 1990. Immunization with a peptide having both T cell and conformationally restricted B cell epitopes elicits neutralizing antisera against a snake neurotoxin. J. Immunol. 145:4214-4221.
    • (1990) J. Immunol. , vol.145 , pp. 4214-4221
    • Léonetti, M.1    Pillet, L.2    Maillère, B.3    Lamthanh, H.4    Frachon, P.5    Couderc, J.6    Ménez, A.7
  • 24
    • 0030862924 scopus 로고    scopus 로고
    • HIV-1 Tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region
    • Chang, H. C., F. Samaniego, B. C. Nair, L. Buonaguro, and B. Ensoli. 1997. HIV-1 Tat protein exits from cells via a leaderless secretory pathway and binds to extracellular matrix-associated heparan sulfate proteoglycans through its basic region. AIDS 11:1421-1431.
    • (1997) AIDS , vol.11 , pp. 1421-1431
    • Chang, H.C.1    Samaniego, F.2    Nair, B.C.3    Buonaguro, L.4    Ensoli, B.5
  • 25
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • Tyagi, M., M. Rusnati, M. Presta, and M. Giacca. 2001. Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans. J. Biol. Chem. 276:3254-3261.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 26
    • 0031029940 scopus 로고    scopus 로고
    • Heparin and heparan sulfate bind to snake cardiotoxin. Sulfated oligosaccharidesasapotential target for cardiotoxin action
    • Patel, H. V., A. A. Vyas, K. A. Vyas, Y. S. Liu, C. M. Chiang, L. M. Chi, and W. Wu. 1997. Heparin and heparan sulfate bind to snake cardiotoxin. Sulfated oligosaccharidesasapotential target for cardiotoxin action. J. Biol. Chem. 272:1484-1492.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1484-1492
    • Patel, H.V.1    Vyas, A.A.2    Vyas, K.A.3    Liu, Y.S.4    Chiang, C.M.5    Chi, L.M.6    Wu, W.7
  • 27
    • 0344417125 scopus 로고    scopus 로고
    • Presentation of antigen in immune complexes is boosted by soluble bacterial immunoglobulin binding proteins
    • Léonetti, M., J. Galon, R. Thai, C. Sautès-Fridman, G. Moine, and A. Ménez. 1999. Presentation of antigen in immune complexes is boosted by soluble bacterial immunoglobulin binding proteins. J. Exp. Med. 189:1217-1228.
    • (1999) J. Exp. Med. , vol.189 , pp. 1217-1228
    • Léonetti, M.1    Galon, J.2    Thai, R.3    Sautès-Fridman, C.4    Moine, G.5    Ménez, A.6
  • 28
    • 33645637052 scopus 로고    scopus 로고
    • HIV-1 Tat raises an adjuvant-free humoral immune response controlled by its core region and its ability to form cysteine-mediated oligomers
    • Kittiworakarn, J., A. Lecoq, G. Moine, R. Thai, E. Lajeunesse, P. Drevet, C. Vidaud, A. Ménez, and M. Léonetti. 2006. HIV-1 Tat raises an adjuvant-free humoral immune response controlled by its core region and its ability to form cysteine-mediated oligomers. J. Biol. Chem. 281:3105-3115.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3105-3115
    • Kittiworakarn, J.1    Lecoq, A.2    Moine, G.3    Thai, R.4    Lajeunesse, E.5    Drevet, P.6    Vidaud, C.7    Ménez, A.8    Léonetti, M.9
  • 30
    • 0028792130 scopus 로고
    • Probing immunogenicity of a T cell epitope by L-alanine and D-amino acidscanning
    • Maillère, B., G. Mourier, J. Cotton, M. Hervé, S. Leroy, and A. Ménez. 1995. Probing immunogenicity of a T cell epitope by L-alanine and D-amino acidscanning. Mol. Immunol. 32:1073-1080.
    • (1995) Mol. Immunol. , vol.32 , pp. 1073-1080
    • Maillère, B.1    Mourier, G.2    Cotton, J.3    Hervé, M.4    Leroy, S.5    Ménez, A.6
  • 32
    • 0032536534 scopus 로고    scopus 로고
    • Type II and III receptors for immunoglobulin G (IgG) control the presentation of different T cell epitopes from single IgG-complexed antigens
    • Amigorena, S., D. Lankar, V. Briken, L. Gapin, M. Viguier, and C. Bonnerot. 1998. Type II and III receptors for immunoglobulin G (IgG) control the presentation of different T cell epitopes from single IgG-complexed antigens. J. Exp. Med. 187:505-515.
    • (1998) J. Exp. Med. , vol.187 , pp. 505-515
    • Amigorena, S.1    Lankar, D.2    Briken, V.3    Gapin, L.4    Viguier, M.5    Bonnerot, C.6
  • 34
    • 0023974392 scopus 로고
    • Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis
    • Miller, J., J. A. Hatch, S. Simonis, and S. E. Cullen. 1988. Identification of the glycosaminoglycan-attachment site of mouse invariant-chain proteoglycan core protein by site-directed mutagenesis. Proc. Natl. Acad. Sci. USA 85:1369.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1369
    • Miller, J.1    Hatch, J.A.2    Simonis, S.3    Cullen, S.E.4
  • 35
    • 0027282460 scopus 로고
    • The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44
    • Naujokas, M. F., M. Morin, M. S. Anderson, M. Peterson, and J. Miller. 1993. The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44. Cell 74:257-268.
    • (1993) Cell. , vol.74 , pp. 257-268
    • Naujokas, M.F.1    Morin, M.2    Anderson, M.S.3    Peterson, M.4    Miller, J.5
  • 36
    • 0034681122 scopus 로고    scopus 로고
    • Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a gammainterferon-inducible lysosomal thiol reductase (GILT)
    • Arunachalam, B., U. T. Phan, H. J. Geuze, and P. Cresswell. 2000. Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gammainterferon-inducible lysosomal thiol reductase (GILT). Proc. Natl. Acad. Sci. USA 97:745-750.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 745-750
    • Arunachalam, B.1    Phan, U.T.2    Geuze, H.J.3    Cresswell, P.4
  • 38
    • 33746111184 scopus 로고    scopus 로고
    • Polyarginine-mediated protein delivery to dendritic cells presents antigen more efficiently onto MHC class I and class II and elicits superior antitumor immunity
    • Mitsui, H., T. Inozume, R. Kitamura, N. Shibagaki, and S. Shimada. 2006. Polyarginine-mediated protein delivery to dendritic cells presents antigen more efficiently onto MHC class I and class II and elicits superior antitumor immunity. J. Invest. Dermatol. 126:1804-1812.
    • (2006) J. Invest. Dermatol. , vol.126 , pp. 1804-1812
    • Mitsui, H.1    Inozume, T.2    Kitamura, R.3    Shibagaki, N.4    Shimada, S.5
  • 40
    • 33646236541 scopus 로고    scopus 로고
    • Oligoarginine vectors for intracellular delivery: Design and cellularuptake mechanisms
    • Futaki, S. 2006. Oligoarginine vectors for intracellular delivery: design and cellularuptake mechanisms. Biopolymers 84:241-249.
    • (2006) Biopolymers , vol.84 , pp. 241-249
    • Futaki, S.1
  • 41
    • 51549100883 scopus 로고    scopus 로고
    • Immunodominance of CD4T cellstoforeign antigens ispeptide intrinsic and independent of molecular context: Implications for vaccine design
    • Weaver, J. M., C. A. Lazarski, K. A. Richards, F. A. Chaves, S. A. Jenks, P. R. Menges, and A. J. Sant. 2008. Immunodominance of CD4T cellstoforeign antigens ispeptide intrinsic and independent of molecular context: implications for vaccine design. J. Immunol. 181:3039-3048.
    • (2008) J. Immunol. , vol.181 , pp. 3039-3048
    • Weaver, J.M.1    Lazarski, C.A.2    Richards, K.A.3    Chaves, F.A.4    Jenks, S.A.5    Menges, P.R.6    Sant, A.J.7
  • 42
    • 14844340568 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    • Delamarre, L., M. Pack, H. Chang, I. Mellman, and E. S. Trombetta. 2005. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science 307:1630-1634.
    • (2005) Science , vol.307 , pp. 1630-1634
    • Delamarre, L.1    Pack, M.2    Chang, H.3    Mellman, I.4    Trombetta, E.S.5
  • 43
    • 33744500203 scopus 로고    scopus 로고
    • Cell surface proteoglycan expression during maturation of human monocytesderived dendritic cells and macrophages
    • Wegrowski, Y., A. L. Milard, G. Kotlarz, E. Toulmonde, F. X. Maquart, and J. Bernard. 2006. Cell surface proteoglycan expression during maturation of human monocytesderived dendritic cells and macrophages. Clin. Exp. Immunol. 144:485-493.
    • (2006) Clin. Exp. Immunol. , vol.144 , pp. 485-493
    • Wegrowski, Y.1    Milard, A.L.2    Kotlarz, G.3    Toulmonde, E.4    Maquart, F.X.5    Bernard, J.6
  • 44
    • 33846548566 scopus 로고    scopus 로고
    • Structural view of glycosaminoglycan-protein interactions
    • Imberty, A., H. Lortat-Jacob, and S. Pérez. 2007. Structural view of glycosaminoglycan-protein interactions. Carbohydr. Res. 342:430-439.
    • (2007) Carbohydr. Res. , vol.342 , pp. 430-439
    • Imberty, A.1    Lortat-Jacob, H.2    Pérez, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.