메뉴 건너뛰기




Volumn 290, Issue 27, 2015, Pages 16759-16771

A novel mechanism for binding of galactose-terminated glycans by the C-type carbohydrate recognition domain in blood dendritic cell antigen 2

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; EPITOPES; POLYSACCHARIDES;

EID: 84936803679     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.660613     Document Type: Article
Times cited : (36)

References (41)
  • 1
    • 0034547923 scopus 로고    scopus 로고
    • BDCA-2, BDCA-3, and BDCA-4: Three markers for distinct subsets of dendritic cells in human peripheral blood
    • Dzionek, A., Fuchs, A., Schmidt, P., Cremer, S., Zysk, M., Miltenyi, S., Buck, D. W., and Schmitz, J. (2000) BDCA-2, BDCA-3, and BDCA-4: Three markers for distinct subsets of dendritic cells in human peripheral blood. J. Immunol. 165, 6037-6046.
    • (2000) J. Immunol , vol.165 , pp. 6037-6046
    • Dzionek, A.1    Fuchs, A.2    Schmidt, P.3    Cremer, S.4    Zysk, M.5    Miltenyi, S.6    Buck, D.W.7    Schmitz, J.8
  • 3
  • 4
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis, W. I., Taylor, M. E., and Drickamer, K. (1998) The C-type lectin superfamily in the immune system. Immunol. Rev. 163, 19-34.
    • (1998) Immunol. Rev. , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 7
    • 84876117810 scopus 로고    scopus 로고
    • C-Type lectin-like receptors of the dectin-1 cluster: Ligands and signaling pathways
    • Plato, A., Willment, J. A., and Brown, G. D. (2013) C-Type lectin-like receptors of the dectin-1 cluster: ligands and signaling pathways. Int. Rev. Immunol. 32, 134-156.
    • (2013) Int. Rev. Immunol , vol.32 , pp. 134-156
    • Plato, A.1    Willment, J.A.2    Brown, G.D.3
  • 8
    • 37549055771 scopus 로고    scopus 로고
    • CD303 (BDCA-2) signals in plasmacytoid dendritic cells via a BCR-like signalosome involving Syk, Slp65 and PLCγ2
    • Röck, J., Schneider, E., Grün, J. R., Grützkau, A., Küppers, R., Schmitz, J., and Winkels, G. (2007) CD303 (BDCA-2) signals in plasmacytoid dendritic cells via a BCR-like signalosome involving Syk, Slp65 and PLCγ2. Eur. J. Immunol. 37, 3564-3575.
    • (2007) Eur. J. Immunol , vol.37 , pp. 3564-3575
    • Röck, J.1    Schneider, E.2    Grün, J.R.3    Grützkau, A.4    Küppers, R.5    Schmitz, J.6    Winkels, G.7
  • 9
    • 35649000957 scopus 로고    scopus 로고
    • BDCA2/FceR1g complex signals through a novel BCR-like pathway in human plasmcytoid dendritic cells
    • Cao, W., Zhang, L., Rosen, D. B., Bover, L., Watanabe, G., Bao, M., Lanier, L. L., and Liu, Y. J. (2007) BDCA2/FceR1g complex signals through a novel BCR-like pathway in human plasmcytoid dendritic cells. PLoS Biol. 5, e248.
    • (2007) PLoS Biol. , vol.5 , pp. e248
    • Cao, W.1    Zhang, L.2    Rosen, D.B.3    Bover, L.4    Watanabe, G.5    Bao, M.6    Lanier, L.L.7    Liu, Y.J.8
  • 10
    • 77956178739 scopus 로고    scopus 로고
    • BDCA-2 signaling inhibits TLR-9-agonist-induced plasmacytoid dendritic cell activation and antigen presentation
    • Jähn, P. S., Zänker, K. S., Schmitz, J., and Dzionek, A. (2010) BDCA-2 signaling inhibits TLR-9-agonist-induced plasmacytoid dendritic cell activation and antigen presentation. Cell. Immunol. 265, 15-22.
    • (2010) Cell. Immunol , vol.265 , pp. 15-22
    • Jähn, P.S.1    Zänker, K.S.2    Schmitz, J.3    Dzionek, A.4
  • 11
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • Drickamer, K. (1992) Engineering galactose-binding activity into a C-type mannose-binding protein. Nature 360, 183-186.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 12
    • 79952555821 scopus 로고    scopus 로고
    • Survey of immune-related mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities
    • Lee, R. T., Hsu, T. L., Huang, S. K., Hsieh, S. L., Wong, C. H., and Lee, Y. C. (2011) Survey of immune-related mannose/fucose-binding C-type lectin receptors reveals widely divergent sugar-binding specificities. Glycobiology 21, 512-520.
    • (2011) Glycobiology , vol.21 , pp. 512-520
    • Lee, R.T.1    Hsu, T.L.2    Huang, S.K.3    Hsieh, S.L.4    Wong, C.H.5    Lee, Y.C.6
  • 14
    • 84902166527 scopus 로고    scopus 로고
    • Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain- swapped dimer
    • Nagae, M., Ikeda, A., Kitago, Y., Matsumoto, N., Yamamoto, K., and Yamaguchi, Y. (2014) Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain- swapped dimer. Proteins 82, 1512-1518.
    • (2014) Proteins , vol.82 , pp. 1512-1518
    • Nagae, M.1    Ikeda, A.2    Kitago, Y.3    Matsumoto, N.4    Yamamoto, K.5    Yamaguchi, Y.6
  • 15
    • 84863422622 scopus 로고    scopus 로고
    • An efficient approach for large-scale production of sialylglycopeptides from egg yolks
    • Zou, Y., Wu, Z., Chen, L., Liu, X., Gu, G., Xue, M., Wang, P. G., and Chen, M. (2012) An efficient approach for large-scale production of sialylglycopeptides from egg yolks. J. Carbohydr. Chem. 31, 436-446.
    • (2012) J. Carbohydr. Chem , vol.31 , pp. 436-446
    • Zou, Y.1    Wu, Z.2    Chen, L.3    Liu, X.4    Gu, G.5    Xue, M.6    Wang, P.G.7    Chen, M.8
  • 16
    • 39549094455 scopus 로고    scopus 로고
    • Analysis of oligosaccharide negative charge by anionexchange chromatography
    • Varki, A. (2001) Analysis of oligosaccharide negative charge by anionexchange chromatography. Curr. Prot. Mol. Biol. 17, 2021-2027.
    • (2001) Curr. Prot. Mol. Biol , vol.17 , pp. 2021-2027
    • Varki, A.1
  • 17
    • 0016754024 scopus 로고
    • Characterization studies on a new lectin found in seed of Vicia ervilia
    • Fornstedt, N., and Porath, J. (1975) Characterization studies on a new lectin found in seed of Vicia ervilia. FEBS Lett. 57, 187-191.
    • (1975) FEBS Lett , vol.57 , pp. 187-191
    • Fornstedt, N.1    Porath, J.2
  • 18
    • 0025021471 scopus 로고
    • Primary structure and functional expression from complementary DNA of a human interleukin-1 receptor antagonist
    • Eisenberg, S. P., Evans, R. J., Arend, W. P., Verderber, E., Brewer, M. T., Hannum, C. H., and Thompson, R. C. (1990) Primary structure and functional expression from complementary DNA of a human interleukin-1 receptor antagonist. Nature 343, 341-346.
    • (1990) Nature , vol.343 , pp. 341-346
    • Eisenberg, S.P.1    Evans, R.J.2    Arend, W.P.3    Verderber, E.4    Brewer, M.T.5    Hannum, C.H.6    Thompson, R.C.7
  • 19
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz, P. J. (1993) Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology 11, 1138-1143.
    • (1993) Biotechnology , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 20
    • 45549098904 scopus 로고    scopus 로고
    • Directed mutagenesis using the polymerase chain reaction
    • Cormack, B. (2001) Directed mutagenesis using the polymerase chain reaction. Curr. Protoc. Neurosci. 4, 11.
    • (2001) Curr. Protoc. Neurosci , vol.4 , pp. 11
    • Cormack, B.1
  • 21
    • 84941104671 scopus 로고    scopus 로고
    • Defining the conformation of human mincle that interacts with mycobacterial trehalose dimycolate
    • Jégouzo, S. A., Harding, E. C., Acton, O., Rex, M. J., Fadden, A. J., Taylor, M. E., and Drickamer, K. (2014) Defining the conformation of human mincle that interacts with mycobacterial trehalose dimycolate. Glycobiology 24, 1291-1300.
    • (2014) Glycobiology , vol.24 , pp. 1291-1300
    • Jégouzo, S.A.1    Harding, E.C.2    Acton, O.3    Rex, M.J.4    Fadden, A.J.5    Taylor, M.E.6    Drickamer, K.7
  • 23
    • 77956127888 scopus 로고
    • The preparation of 131I-labelled human growth hormone of high specific radioactivity
    • Greenwood, F. C., Hunter, W. M., and Glover, J. S. (1963) The preparation of 131I-labelled human growth hormone of high specific radioactivity. Biochem. J. 89, 114-123.
    • (1963) Biochem. J. , vol.89 , pp. 114-123
    • Greenwood, F.C.1    Hunter, W.M.2    Glover, J.S.3
  • 27
  • 30
    • 2942687010 scopus 로고    scopus 로고
    • Phylogenetic expression of Galα1-4Gal on avian glycoproteins: Glycan differentiation inscribed in the early history of modern birds
    • Suzuki, N., Laskowski, M. Jr., and Lee, Y. C. (2004) Phylogenetic expression of Galα1-4Gal on avian glycoproteins: glycan differentiation inscribed in the early history of modern birds. Proc. Natl. Acad. Sci. U.S.A. 101, 9023-9028.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 9023-9028
    • Suzuki, N.1    Laskowski, M.2    Lee, Y.C.3
  • 31
    • 0025906415 scopus 로고
    • Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A): Homology of binding site architecture with mammalian and chicken hepatic lectins
    • Lee, R. T., Ichikawa, Y., Fay, M., Drickamer, K., Shao, M.-C., and Lee, Y. C. (1991) Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A): homology of binding site architecture with mammalian and chicken hepatic lectins. J. Biol. Chem. 266, 4810-4815.
    • (1991) J. Biol. Chem , vol.266 , pp. 4810-4815
    • Lee, R.T.1    Ichikawa, Y.2    Fay, M.3    Drickamer, K.4    Shao, M.-C.5    Lee, Y.C.6
  • 32
    • 0037013245 scopus 로고    scopus 로고
    • Orientation of bound ligands in mannose-binding proteins: Implications of multivalent ligand recognition
    • Ng, K. K., Kolatkar, A. R., Park-Snyder, S., Feinberg, H., Clark, D. A., Drickamer, K., and Weis, W. I. (2002) Orientation of bound ligands in mannose-binding proteins: Implications of multivalent ligand recognition. J. Biol. Chem. 277, 16088-16095.
    • (2002) J. Biol. Chem , vol.277 , pp. 16088-16095
    • Ng, K.K.1    Kolatkar, A.R.2    Park-Snyder, S.3    Feinberg, H.4    Clark, D.A.5    Drickamer, K.6    Weis, W.I.7
  • 33
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd, P. M., and Dwek, R. A. (1997) Glycosylation: heterogeneity and the 3D structure of proteins. Crit. Rev. Biochem. Mol. Biol. 32, 1-100.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 34
    • 0034647695 scopus 로고    scopus 로고
    • Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor
    • Feinberg, H., Park-Snyder, S., Kolatkar, A. R., Heise, C. T., Taylor, M. E., and Weis, W. I. (2000) Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor. J. Biol. Chem. 275, 21539-21548.
    • (2000) J. Biol. Chem , vol.275 , pp. 21539-21548
    • Feinberg, H.1    Park-Snyder, S.2    Kolatkar, A.R.3    Heise, C.T.4    Taylor, M.E.5    Weis, W.I.6
  • 35
    • 0030979409 scopus 로고    scopus 로고
    • Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains
    • Mizuno, H., Fujimoto, Z., Koizumi, M., Kano, H., Atoda, H., and Morita, T. (1997) Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains. Nat. Struct. Biol. 4, 438-441.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 438-441
    • Mizuno, H.1    Fujimoto, Z.2    Koizumi, M.3    Kano, H.4    Atoda, H.5    Morita, T.6
  • 36
    • 0029917167 scopus 로고    scopus 로고
    • Structural basis of galactose recognition by C-type animal lectins
    • Kolatkar, A. R., and Weis, W. I. (1996) Structural basis of galactose recognition by C-type animal lectins. J. Biol. Chem. 271, 6679-6685.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6679-6685
    • Kolatkar, A.R.1    Weis, W.I.2
  • 37
    • 0034634584 scopus 로고    scopus 로고
    • Mechanism of pH-dependent N-acetylgalactosamine binding to a functional mimic of the hepatic asialoglycoprotein receptor
    • Feinberg, H., Torgersen, D., Drickamer, K., and Weis, W. I. (2000) Mechanism of pH-dependent N-acetylgalactosamine binding to a functional mimic of the hepatic asialoglycoprotein receptor. J. Biol. Chem. 275, 35176-35184.
    • (2000) J. Biol. Chem , vol.275 , pp. 35176-35184
    • Feinberg, H.1    Torgersen, D.2    Drickamer, K.3    Weis, W.I.4
  • 38
    • 34447118190 scopus 로고    scopus 로고
    • Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis x by a novel mechanism
    • Feinberg, H., Taylor, M. E., and Weis, W. I. (2007) Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis x by a novel mechanism. J. Biol. Chem. 282, 17250-17258.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17250-17258
    • Feinberg, H.1    Taylor, M.E.2    Weis, W.I.3
  • 39
    • 84888357760 scopus 로고    scopus 로고
    • Recognition of bisecting N-acetylglucosamine: Structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2
    • Nagae, M., Yamanaka, K., Hanashima, S., Ikeda, A., Morita-Matsumoto, K., Satoh, T., Matsumoto, N., Yamamoto, K., and Yamaguchi, Y. (2013) Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2. J. Biol. Chem. 288, 33598-33610.
    • (2013) J. Biol. Chem , vol.288 , pp. 33598-33610
    • Nagae, M.1    Yamanaka, K.2    Hanashima, S.3    Ikeda, A.4    Morita-Matsumoto, K.5    Satoh, T.6    Matsumoto, N.7    Yamamoto, K.8    Yamaguchi, Y.9
  • 40
    • 0029731813 scopus 로고    scopus 로고
    • Fc receptors and their interactions with immunoglobulins
    • Raghavan, M., and Bjorkman, P. J. (1996) Fc receptors and their interactions with immunoglobulins. Annu. Rev. Cell Dev. Biol. 12, 181-220.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 181-220
    • Raghavan, M.1    Bjorkman, P.J.2
  • 41
    • 84866533031 scopus 로고    scopus 로고
    • Distinct roles of myeloid and plasmacytoid dendritic cells in systemic lupus erythematosus
    • Chan, V. S., Nie, Y. J., Shen, N., Yan, S., Mok, M. Y., and Lau, C. S. (2012) Distinct roles of myeloid and plasmacytoid dendritic cells in systemic lupus erythematosus. Autoimmun. Rev. 11, 890-897.
    • (2012) Autoimmun. Rev. , vol.11 , pp. 890-897
    • Chan, V.S.1    Nie, Y.J.2    Shen, N.3    Yan, S.4    Mok, M.Y.5    Lau, C.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.