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Volumn 579, Issue 27, 2005, Pages 6159-6168

Interactions of DC-SIGN with Mac-1 and CEACAM1 regulate contact between dendritic cells and neutrophils

Author keywords

DC maturation; DC SIGN; Dendritic cells; Glycosylation; Neutrophils

Indexed keywords

CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 1; CD11B ANTIGEN; CD209 ANTIGEN; LECTIN; LIGAND;

EID: 27544447389     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.09.089     Document Type: Article
Times cited : (90)

References (53)
  • 2
    • 0027301114 scopus 로고
    • Expression and regulation of human neutrophil-derived macrophage inflammatory protein-1-α
    • T. Kasama, R.M. Strieter, T.J. Standiford, M.D. Burdick, and S.L. Kunkel Expression and regulation of human neutrophil-derived macrophage inflammatory protein-1-α J. Exp. Med. 178 1993 63 72
    • (1993) J. Exp. Med. , vol.178 , pp. 63-72
    • Kasama, T.1    Strieter, R.M.2    Standiford, T.J.3    Burdick, M.D.4    Kunkel, S.L.5
  • 4
    • 0033844287 scopus 로고    scopus 로고
    • Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells
    • D. Yang, Q. Chen, O. Chertov, and J.J. Oppenheim Human neutrophil defensins selectively chemoattract naive T and immature dendritic cells J. Leukoc. Biol. 68 2000 9 14
    • (2000) J. Leukoc. Biol. , vol.68 , pp. 9-14
    • Yang, D.1    Chen, Q.2    Chertov, O.3    Oppenheim, J.J.4
  • 5
    • 0037378907 scopus 로고    scopus 로고
    • -/- mice delays clearance of gastric Helicobacter infection and decreases the Th1 immune response to Helicobacter
    • -/- mice delays clearance of gastric Helicobacter infection and decreases the Th1 immune response to Helicobacter J. Immunol. 170 2003 3782 3789
    • (2003) J. Immunol. , vol.170 , pp. 3782-3789
    • Ismail, H.F.1    Fick, P.2    Zhang, J.3    Lynch, R.G.4    Berg, D.J.5
  • 8
    • 18244389671 scopus 로고    scopus 로고
    • Neutrophils mediate immune modulation of dendritic cells through glycosylation-dependent interactions between Mac-1 and DC-SIGN
    • K.P.J.M. van Gisbergen, M. Sanchez-Hernandez, T.B.H. Geijtenbeek, and Y. van Kooyk Neutrophils mediate immune modulation of dendritic cells through glycosylation-dependent interactions between Mac-1 and DC-SIGN J. Exp. Med. 201 2005 1281 1292
    • (2005) J. Exp. Med. , vol.201 , pp. 1281-1292
    • Van Gisbergen, K.P.J.M.1    Sanchez-Hernandez, M.2    Geijtenbeek, T.B.H.3    Van Kooyk, Y.4
  • 9
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • J. Banchereau, and R.M. Steinman Dendritic cells and the control of immunity Nature 392 1998 245 252
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 10
    • 0345690207 scopus 로고    scopus 로고
    • Cross-talk in the innate immune system: Neutrophils instruct recruitment and activation of dendritic cells during microbial infection
    • S. Bennouna, S.K. Bliss, T.J. Curiel, and E.Y. Denkers Cross-talk in the innate immune system: Neutrophils instruct recruitment and activation of dendritic cells during microbial infection J. Immunol. 171 2003 6052 6058
    • (2003) J. Immunol. , vol.171 , pp. 6052-6058
    • Bennouna, S.1    Bliss, S.K.2    Curiel, T.J.3    Denkers, E.Y.4
  • 11
    • 0037442109 scopus 로고    scopus 로고
    • Cutting edge: Carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells
    • B.J. Appelmelk, I. van Die, S.J. van Vliet, C.M.J.E. Vandenbroucke- Grauls, T.B.H. Geijtenbeek, and Y. van Kooyk Cutting edge: Carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells J. Immunol. 170 2003 1635 1639
    • (2003) J. Immunol. , vol.170 , pp. 1635-1639
    • Appelmelk, B.J.1    Van Die, I.2    Van Vliet, S.J.3    Vandenbroucke-Grauls, C.M.J.E.4    Geijtenbeek, T.B.H.5    Van Kooyk, Y.6
  • 12
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • H. Feinberg, D.A. Mitchell, K. Drickamer, and W.I. Weis Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR Science 294 2001 2163 2166
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 17
    • 0022357790 scopus 로고
    • Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA-1, Mo-1 and p150,95
    • G.D. Keizer, J. Borst, C.G. Figdor, H. Spits, F. Miedema, C. Terhorst, and J.E. de Vries Biochemical and functional characteristics of the human leukocyte membrane antigen family LFA-1, Mo-1 and p150,95 Eur. J. Immunol. 15 1985 1142 1148
    • (1985) Eur. J. Immunol. , vol.15 , pp. 1142-1148
    • Keizer, G.D.1    Borst, J.2    Figdor, C.G.3    Spits, H.4    Miedema, F.5    Terhorst, C.6    De Vries, J.E.7
  • 18
    • 0037192786 scopus 로고    scopus 로고
    • Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1
    • T.B.H. Geijtenbeek, G.C.F. van Duijnhoven, S.J. van Vliet, E. Krieger, G. Vriend, C.G. Figdor, and Y. van Kooyk Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1 J. Biol. Chem. 277 2002 11314 11320
    • (2002) J. Biol. Chem. , vol.277 , pp. 11314-11320
    • Geijtenbeek, T.B.H.1    Van Duijnhoven, G.C.F.2    Van Vliet, S.J.3    Krieger, E.4    Vriend, G.5    Figdor, C.G.6    Van Kooyk, Y.7
  • 22
    • 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 down-regulated by tumor-necrosis-factor-α
    • F. Sallusto, and A. Lanzavecchia Efficient presentation of soluble-antigen by cultured human dendritic cells is maintained by granulocyte-macrophage colony-stimulating factor plus interleukin-4 and down-regulated by tumor-necrosis-factor-α J. Exp. Med. 179 1994 1109 1118
    • (1994) J. Exp. Med. , vol.179 , pp. 1109-1118
    • Sallusto, F.1    Lanzavecchia, A.2
  • 24
    • 0020549690 scopus 로고
    • Marker of peripheral blood granulocytes and monocytes of man recognized by two monoclonal antibodies VEP8 and VEP9 involves the trisaccharide 3-fucosyl-N-acetyllactosamine
    • H.C. Gooi, S.J. Thorpe, E.F. Hounsell, H. Rumpold, D. Kraft, O. Forster, and T. Feizi Marker of peripheral blood granulocytes and monocytes of man recognized by two monoclonal antibodies VEP8 and VEP9 involves the trisaccharide 3-fucosyl-N-acetyllactosamine Eur. J. Immunol. 13 1983 306 312
    • (1983) Eur. J. Immunol. , vol.13 , pp. 306-312
    • Gooi, H.C.1    Thorpe, S.J.2    Hounsell, E.F.3    Rumpold, H.4    Kraft, D.5    Forster, O.6    Feizi, T.7
  • 25
    • 0023193152 scopus 로고
    • Monoclonal antibodies that recognize lacto-N-fucopentaose III (CD15) react with the adhesion-promoting glycoprotein family (LFA-1/Mac-1/Gp 150,95) and Cr-1 on human neutrophils
    • K.M. Skubitz, and R.W. Snook Monoclonal antibodies that recognize lacto-N-fucopentaose III (CD15) react with the adhesion-promoting glycoprotein family (LFA-1/Mac-1/Gp 150,95) and Cr-1 on human neutrophils J. Immunol. 139 1987 1631 1639
    • (1987) J. Immunol. , vol.139 , pp. 1631-1639
    • Skubitz, K.M.1    Snook, R.W.2
  • 26
  • 27
    • 0028821581 scopus 로고
    • Molecular cloning and expression of carcinoembryonic antigen gene family members
    • J.A. Thompson Molecular cloning and expression of carcinoembryonic antigen gene family members Tumour Biol. 16 1995 10 16
    • (1995) Tumour Biol. , vol.16 , pp. 10-16
    • Thompson, J.A.1
  • 28
    • 0028861654 scopus 로고
    • Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas
    • S.T. Wong-Madden, and D. Landry Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas Glycobiology 5 1995 19 28
    • (1995) Glycobiology , vol.5 , pp. 19-28
    • Wong-Madden, S.T.1    Landry, D.2
  • 29
    • 0035283315 scopus 로고    scopus 로고
    • Is there a role for CEA in innate immunity in the colon?
    • S. Hammarstrom, and V. Baranov Is there a role for CEA in innate immunity in the colon? Trends Microbiol. 9 2001 119 125
    • (2001) Trends Microbiol. , vol.9 , pp. 119-125
    • Hammarstrom, S.1    Baranov, V.2
  • 30
    • 0031772640 scopus 로고    scopus 로고
    • Biliary glycoprotein (CD66a), a cell adhesion molecule of the immunoglobulin superfamily, on human lymphocytes: Structure, expression and involvement in T cell activation
    • R. Kammerer, S. Hahn, B.B. Singer, J.S. Luo, and S. von Kleist Biliary glycoprotein (CD66a), a cell adhesion molecule of the immunoglobulin superfamily, on human lymphocytes: structure, expression and involvement in T cell activation Eur. J. Immunol. 28 1998 3664 3674
    • (1998) Eur. J. Immunol. , vol.28 , pp. 3664-3674
    • Kammerer, R.1    Hahn, S.2    Singer, B.B.3    Luo, J.S.4    Von Kleist, S.5
  • 32
    • 0034664758 scopus 로고    scopus 로고
    • DC-SIGN; A related gene, DC-SIGNR; And CD23 form a cluster on 19p13
    • E.J. Soilleux, R. Barten, and J. Trowsdale DC-SIGN; a related gene, DC-SIGNR; and CD23 form a cluster on 19p13 J. Immunol. 165 2000 2937 2942
    • (2000) J. Immunol. , vol.165 , pp. 2937-2942
    • Soilleux, E.J.1    Barten, R.2    Trowsdale, J.3
  • 35
    • 0035844163 scopus 로고    scopus 로고
    • CD15 expression in mature granulocytes is determined by α1,3-fucosyltransferase IX, but in promyelocytes and monocytes by α1,3-fucosyltransferase IV
    • F. Nakayama, S. Nishihara, H. Iwasaki, T. Kudo, R. Okubo, M. Kaneko, M. Nakamura, M. Karube, K. Sasaki, and H. Narimatsu CD15 expression in mature granulocytes is determined by α1,3-fucosyltransferase IX, but in promyelocytes and monocytes by α1,3-fucosyltransferase IV J. Biol. Chem. 276 2001 16100 16106
    • (2001) J. Biol. Chem. , vol.276 , pp. 16100-16106
    • Nakayama, F.1    Nishihara, S.2    Iwasaki, H.3    Kudo, T.4    Okubo, R.5    Kaneko, M.6    Nakamura, M.7    Karube, M.8    Sasaki, K.9    Narimatsu, H.10
  • 37
    • 0037089660 scopus 로고    scopus 로고
    • Carcinoembryonic antigen as a target for therapeutic anticancer vaccines: A review
    • N.L. Berinstein Carcinoembryonic antigen as a target for therapeutic anticancer vaccines: a review J. Clin. Oncol. 20 2002 2197 2207
    • (2002) J. Clin. Oncol. , vol.20 , pp. 2197-2207
    • Berinstein, N.L.1
  • 38
  • 39
    • 0028819437 scopus 로고
    • Carbohydrate structures of a normal counterpart of the carcinoembryonic antigen produced by colon epithelial cells of normal adults
    • K. Fukushima, T. Ohkura, M. Kanai, M. Kuroki, Y. Matsuoka, A. Kobata, and K. Yamashita Carbohydrate structures of a normal counterpart of the carcinoembryonic antigen produced by colon epithelial cells of normal adults Glycobiology 5 1995 105 115
    • (1995) Glycobiology , vol.5 , pp. 105-115
    • Fukushima, K.1    Ohkura, T.2    Kanai, M.3    Kuroki, M.4    Matsuoka, Y.5    Kobata, A.6    Yamashita, K.7
  • 40
    • 0022382629 scopus 로고
    • Carbohydrate determinants associated with carcinoembryonic antigen (CEA)
    • E.J. Nichols, R. Kannagi, S.I. Hakomori, M.J. Krantz, and A. Fuks Carbohydrate determinants associated with carcinoembryonic antigen (CEA) J. Immunol. 135 1985 1911 1913
    • (1985) J. Immunol. , vol.135 , pp. 1911-1913
    • Nichols, E.J.1    Kannagi, R.2    Hakomori, S.I.3    Krantz, M.J.4    Fuks, A.5
  • 41
    • 0023221836 scopus 로고
    • Structural studies of the carbohydrate moieties of carcinoembryonic antigens
    • K. Yamashita, K. Totani, M. Kuroki, Y. Matsuoka, I. Ueda, and A. Kobata Structural studies of the carbohydrate moieties of carcinoembryonic antigens Cancer Res. 47 1987 3451 3459
    • (1987) Cancer Res. , vol.47 , pp. 3451-3459
    • Yamashita, K.1    Totani, K.2    Kuroki, M.3    Matsuoka, Y.4    Ueda, I.5    Kobata, A.6
  • 42
    • 21344449731 scopus 로고    scopus 로고
    • Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin
    • K.P.J.M. van Gisbergen, C.A. Aarnoudse, G.A. Meijer, T.B.H. Geijtenbeek, and Y. van Kooyk Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin Cancer Res. 65 2005 5935 5944
    • (2005) Cancer Res. , vol.65 , pp. 5935-5944
    • Van Gisbergen, K.P.J.M.1    Aarnoudse, C.A.2    Meijer, G.A.3    Geijtenbeek, T.B.H.4    Van Kooyk, Y.5
  • 43
    • 0032951724 scopus 로고    scopus 로고
    • The carboxyl-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein-tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells
    • M. Huber, L. Izzi, P. Grondin, C. Houde, T. Kunath, A. Veillette, and N. Beauchemin The carboxyl-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein-tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells J. Biol. Chem. 274 1999 335 344
    • (1999) J. Biol. Chem. , vol.274 , pp. 335-344
    • Huber, M.1    Izzi, L.2    Grondin, P.3    Houde, C.4    Kunath, T.5    Veillette, A.6    Beauchemin, N.7
  • 44
    • 0028859572 scopus 로고
    • CD66 family members are associated with tyrosine kinase activity in human neutrophils
    • K.M. Skubitz, K.D. Campbell, K. Ahmed, and A.P. Skubitz CD66 family members are associated with tyrosine kinase activity in human neutrophils J. Immunol. 155 1995 5382 5390
    • (1995) J. Immunol. , vol.155 , pp. 5382-5390
    • Skubitz, K.M.1    Campbell, K.D.2    Ahmed, K.3    Skubitz, A.P.4
  • 46
    • 0029957169 scopus 로고    scopus 로고
    • Role of nonspecific cross-reacting antigen, a CD66 cluster antigen, in activation of human granulocytes
    • M.L. Klein, S.A. McGhee, J. Baranian, L. Stevens, and S.A. Hefta Role of nonspecific cross-reacting antigen, a CD66 cluster antigen, in activation of human granulocytes Infect. Immun. 64 1996 4574 4579
    • (1996) Infect. Immun. , vol.64 , pp. 4574-4579
    • Klein, M.L.1    McGhee, S.A.2    Baranian, J.3    Stevens, L.4    Hefta, S.A.5
  • 47
    • 0029888823 scopus 로고    scopus 로고
    • CD66a, CD66b, CD66c, and CD66d each independently stimulate neutrophils
    • K.M. Skubitz, K.D. Campbell, and A.P. Skubitz CD66a, CD66b, CD66c, and CD66d each independently stimulate neutrophils J. Leukoc. Biol. 60 1996 106 117
    • (1996) J. Leukoc. Biol. , vol.60 , pp. 106-117
    • Skubitz, K.M.1    Campbell, K.D.2    Skubitz, A.P.3
  • 48
    • 0033571388 scopus 로고    scopus 로고
    • Identification of CD66a and CD66b as the major galectin-3 receptor candidates in human neutrophils
    • E. Feuk-Lagerstedt, E.T. Jordan, H. Leffler, C. Dahlgren, and A. Karlsson Identification of CD66a and CD66b as the major galectin-3 receptor candidates in human neutrophils J. Immunol. 163 1999 5592 5598
    • (1999) J. Immunol. , vol.163 , pp. 5592-5598
    • Feuk-Lagerstedt, E.1    Jordan, E.T.2    Leffler, H.3    Dahlgren, C.4    Karlsson, A.5
  • 50
    • 0036135609 scopus 로고    scopus 로고
    • Complementary adhesion molecules promote neutrophil-Kupffer cell interaction and the elimination of bacteria taken up by the liver
    • S.H. Gregory, L.P. Cousens, N. van Rooijen, E.A. Dopp, T.M. Carlos, and E.J. Wing Complementary adhesion molecules promote neutrophil-Kupffer cell interaction and the elimination of bacteria taken up by the liver J. Immunol. 168 2002 308 315
    • (2002) J. Immunol. , vol.168 , pp. 308-315
    • Gregory, S.H.1    Cousens, L.P.2    Van Rooijen, N.3    Dopp, E.A.4    Carlos, T.M.5    Wing, E.J.6
  • 51
    • 0035451091 scopus 로고    scopus 로고
    • Neutrophils process exogenous bacteria via an alternate class I MHC processing pathway for presentation of peptides to T lymphocytes
    • N.S. Potter, and C.V. Harding Neutrophils process exogenous bacteria via an alternate class I MHC processing pathway for presentation of peptides to T lymphocytes J. Immunol. 167 2001 2538 2546
    • (2001) J. Immunol. , vol.167 , pp. 2538-2546
    • Potter, N.S.1    Harding, C.V.2
  • 53
    • 0030965374 scopus 로고    scopus 로고
    • CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes
    • S.D. Gray-Owen, C. Dehio, A. Haude, F. Grunert, and T.F. Meyer CD66 carcinoembryonic antigens mediate interactions between Opa-expressing Neisseria gonorrhoeae and human polymorphonuclear phagocytes EMBO J. 16 1997 3435 3445
    • (1997) EMBO J. , vol.16 , pp. 3435-3445
    • Gray-Owen, S.D.1    Dehio, C.2    Haude, A.3    Grunert, F.4    Meyer, T.F.5


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