메뉴 건너뛰기




Volumn 1721, Issue 1-3, 2005, Pages 152-163

Lectin KM +-induced neutrophil haptotaxis involves binding to laminin

Author keywords

Artocarpus integrifolia; Extracellular matrix; Haptotactic gradient; Laminin; Lectin; Neutrophil haptotaxis

Indexed keywords

ARTOCARPIN; CARBOHYDRATE DERIVATIVE; GLYCAN; GLYCOPROTEIN; LAMININ; LECTIN; MANNOSE; PEROXIDASE; UNCLASSIFIED DRUG;

EID: 11844284789     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.10.012     Document Type: Article
Times cited : (39)

References (58)
  • 1
    • 0025912923 scopus 로고
    • Two-step model of leukocyte endothelial-cell interaction in inflammation: Distinct roles for LECAM-1 and the leukocyte beta-2 integrins in vivo
    • U.H. Von Andrian, J.D. Chambers, L.M. McEvoy, R.F. Bargatze, K.E. Arfors, and E.C. Butcher Two-step model of leukocyte endothelial-cell interaction in inflammation: distinct roles for LECAM-1 and the leukocyte beta-2 integrins in vivo Proc. Natl. Acad. Sci. U. S. A. 88 1991 7538 7542
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7538-7542
    • Von Andrian, U.H.1    Chambers, J.D.2    McEvoy, L.M.3    Bargatze, R.F.4    Arfors, K.E.5    Butcher, E.C.6
  • 2
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • L.A. Lasky Selectins: interpreters of cell-specific carbohydrate information during inflammation Science 258 1992 964 969
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 3
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell-adhesion
    • R.O. Hynes Integrins: versatility, modulation, and signaling in cell-adhesion Cell 69 1992 11 25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 4
    • 0031406966 scopus 로고    scopus 로고
    • Selectins, T-cell rolling and inflammation
    • H. Rossiter, R. Alon, and T.S. Kupper Selectins, T-cell rolling and inflammation Mol. Med. Today 3 1997 214 222
    • (1997) Mol. Med. Today , vol.3 , pp. 214-222
    • Rossiter, H.1    Alon, R.2    Kupper, T.S.3
  • 5
    • 0027248750 scopus 로고
    • PECAM-1 is required for transendothelial migration of leukocytes
    • W.A. Muller, S.A. Weigl, X. Deng, and D.M. Phillips PECAM-1 is required for transendothelial migration of leukocytes J. Exp. Med. 178 1993 449 460
    • (1993) J. Exp. Med. , vol.178 , pp. 449-460
    • Muller, W.A.1    Weigl, S.A.2    Deng, X.3    Phillips, D.M.4
  • 6
    • 0030271572 scopus 로고    scopus 로고
    • Macromolecular organization of basement membranes
    • R. Timpl Macromolecular organization of basement membranes Curr. Opin. Cell Biol. 8 1996 618 624
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 618-624
    • Timpl, R.1
  • 7
    • 0026694563 scopus 로고
    • Endothelial-cell binding of NAP-1/IL-8: Role in neutrophil emigration
    • A. Rot Endothelial-cell binding of NAP-1/IL-8: role in neutrophil emigration Immunol. Today 13 1992 291 294
    • (1992) Immunol. Today , vol.13 , pp. 291-294
    • Rot, A.1
  • 8
    • 0035844184 scopus 로고    scopus 로고
    • Haptotactic migration induced by midkine. Involvement of protein-tyrosine phosphatase zeta, mitogen-activated protein kinase, and phosphatidylinositol 3-kinase
    • M.S. Qi, S. Ikematsu, N. Maeda, K. Ichihara-Tanaka, S. Sakuma, M. Noda, T. Muramatsu, and K. Kadomatsu Haptotactic migration induced by midkine. Involvement of protein-tyrosine phosphatase zeta, mitogen-activated protein kinase, and phosphatidylinositol 3-kinase J. Biol. Chem. 276 2001 15868 15875
    • (2001) J. Biol. Chem. , vol.276 , pp. 15868-15875
    • Qi, M.S.1    Ikematsu, S.2    Maeda, N.3    Ichihara-Tanaka, K.4    Sakuma, S.5    Noda, M.6    Muramatsu, T.7    Kadomatsu, K.8
  • 10
    • 0032491615 scopus 로고    scopus 로고
    • Lysine 58 and histidine 66 at the C-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding
    • L. Chakravarty, L. Rogers, T. Quach, S. Breckenridge, and P.E. Kolattukudy Lysine 58 and histidine 66 at the C-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding J. Biol. Chem. 273 1998 29641 29647
    • (1998) J. Biol. Chem. , vol.273 , pp. 29641-29647
    • Chakravarty, L.1    Rogers, L.2    Quach, T.3    Breckenridge, S.4    Kolattukudy, P.E.5
  • 11
    • 0030892080 scopus 로고    scopus 로고
    • Identification of a glycosaminoglycan-binding site in chemokine macrophage inflammatory protein-1 alpha
    • W. Koopmann, and M.S. Krangel Identification of a glycosaminoglycan- binding site in chemokine macrophage inflammatory protein-1 alpha J. Biol. Chem. 272 1997 10103 10109
    • (1997) J. Biol. Chem. , vol.272 , pp. 10103-10109
    • Koopmann, W.1    Krangel, M.S.2
  • 12
    • 0027408343 scopus 로고
    • Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes
    • Y. Tanaka, D.H. Adams, and S. Shaw Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes Immunol. Today 14 1993 111 115
    • (1993) Immunol. Today , vol.14 , pp. 111-115
    • Tanaka, Y.1    Adams, D.H.2    Shaw, S.3
  • 13
    • 0029060187 scopus 로고
    • The IP-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation
    • A.D. Luster, S.M. Greenberg, and P. Leder The IP-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation J. Exp. Med. 182 1995 219 231
    • (1995) J. Exp. Med. , vol.182 , pp. 219-231
    • Luster, A.D.1    Greenberg, S.M.2    Leder, P.3
  • 18
    • 0029942555 scopus 로고    scopus 로고
    • Galectin-3 promotes adhesion of human neutrophils to laminin
    • I. Kuwabara, and F.T. Liu Galectin-3 promotes adhesion of human neutrophils to laminin J. Immunol. 156 1996 3939 3944
    • (1996) J. Immunol. , vol.156 , pp. 3939-3944
    • Kuwabara, I.1    Liu, F.T.2
  • 19
    • 1542313823 scopus 로고    scopus 로고
    • Galectins as inflammatory mediators
    • J. Almkvist, and A. Karlsson Galectins as inflammatory mediators Glycoconj. J. 19 2004 575 581
    • (2004) Glycoconj. J. , vol.19 , pp. 575-581
    • Almkvist, J.1    Karlsson, A.2
  • 20
    • 0027533286 scopus 로고
    • Neutrophil attractant/activation protein-1 (interleukin-8) induces in vitro neutrophil migration by haptotactic mechanism
    • A. Rot Neutrophil attractant/activation protein-1 (interleukin-8) induces in vitro neutrophil migration by haptotactic mechanism Eur. J. Immunol. 23 1993 303 306
    • (1993) Eur. J. Immunol. , vol.23 , pp. 303-306
    • Rot, A.1
  • 21
    • 0019205258 scopus 로고
    • Neutrophil chemotaxis in response to surface-bound C5A
    • R.O. Webster, B. Zanolari, and P.M. Henson Neutrophil chemotaxis in response to surface-bound C5A Exp. Cell Res. 129 1980 55 62
    • (1980) Exp. Cell Res. , vol.129 , pp. 55-62
    • Webster, R.O.1    Zanolari, B.2    Henson, P.M.3
  • 25
    • 0029166796 scopus 로고
    • Biological characterization of purified macrophage-derived neutrophil chemotactic factor
    • M. Dias-Baruffi, M.C. Roque-Barreira, F.Q Cunha, and S.H. Ferreira Biological characterization of purified macrophage-derived neutrophil chemotactic factor Med. Inflamm. 4 1995 263 269
    • (1995) Med. Inflamm. , vol.4 , pp. 263-269
    • Dias-Baruffi, M.1    Roque-Barreira, M.C.2    Cunha, F.Q.3    Ferreira, S.H.4
  • 28
    • 0020794694 scopus 로고
    • Rapid and sensitive colorimetric method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots
    • J.J. Leary, D.J. Brigati, and D.C. Ward Rapid and sensitive colorimetric method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots Proc. Natl. Acad. Sci. U. S. A. 80 1983 4045 4049
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 4045-4049
    • Leary, J.J.1    Brigati, D.J.2    Ward, D.C.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during assembly of head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0018926427 scopus 로고
    • Rapid quantitation of neutrophil chemotaxis: Use of a polyvinylpyrrolidone-free polycarbonate membrane in a multiwell assembly
    • L. Harvath, W. Falk, and E.J. Leonard Rapid quantitation of neutrophil chemotaxis: use of a polyvinylpyrrolidone-free polycarbonate membrane in a multiwell assembly J. Immunol. Methods 37 1980 39 45
    • (1980) J. Immunol. Methods , vol.37 , pp. 39-45
    • Harvath, L.1    Falk, W.2    Leonard, E.J.3
  • 31
    • 0020588997 scopus 로고
    • Migration by haptotaxis of a Schwann-cell tumor line to the basement membrane glycoprotein Laminin
    • J.B. McCarthy, S.L. Palm, and L.T. Furcht Migration by haptotaxis of a Schwann-cell tumor line to the basement membrane glycoprotein Laminin J. Cell Biol. 97 1983 772 777
    • (1983) J. Cell Biol. , vol.97 , pp. 772-777
    • McCarthy, J.B.1    Palm, S.L.2    Furcht, L.T.3
  • 32
    • 0025797046 scopus 로고
    • The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum
    • A. Kurosaka, A. Yano, N. Itoh, Y. Kuroda, T. Nakagawa, and T. Kawasaki The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum J. Biol. Chem. 266 1991 4168 4172
    • (1991) J. Biol. Chem. , vol.266 , pp. 4168-4172
    • Kurosaka, A.1    Yano, A.2    Itoh, N.3    Kuroda, Y.4    Nakagawa, T.5    Kawasaki, T.6
  • 33
    • 0027942508 scopus 로고
    • Carbohydrate-binding specificity of the B-cell maturation mitogen from Artocarpus integrifolia seeds
    • S. Misquith, P.G. Rani, and A. Surolia Carbohydrate-binding specificity of the B-cell maturation mitogen from Artocarpus integrifolia seeds J. Biol. Chem. 269 1994 30393 30401
    • (1994) J. Biol. Chem. , vol.269 , pp. 30393-30401
    • Misquith, S.1    Rani, P.G.2    Surolia, A.3
  • 34
    • 0021328415 scopus 로고
    • The connective-tissue of the rat lung: Electron immunohistochemical studies
    • J. Gil, and A. Martinez-Hernandez The connective-tissue of the rat lung: electron immunohistochemical studies J. Histochem. Cytochem. 32 1984 230 238
    • (1984) J. Histochem. Cytochem. , vol.32 , pp. 230-238
    • Gil, J.1    Martinez-Hernandez, A.2
  • 35
    • 0025165018 scopus 로고
    • Structure and function of laminin: Anatomy of a multidomain glycoprotein
    • K. Beck, I. Hunter, and J. Engel Structure and function of laminin: anatomy of a multidomain glycoprotein FASEB J. 4 1990 148 160
    • (1990) FASEB J. , vol.4 , pp. 148-160
    • Beck, K.1    Hunter, I.2    Engel, J.3
  • 37
    • 0024393502 scopus 로고
    • Structure of the major concanavalin a reactive oligosaccharides of the extracellular matrix component laminin
    • R.N. Knibbs, F. Perini, and I.J. Goldstein Structure of the major concanavalin A reactive oligosaccharides of the extracellular matrix component laminin Biochemistry 28 1989 6379 6392
    • (1989) Biochemistry , vol.28 , pp. 6379-6392
    • Knibbs, R.N.1    Perini, F.2    Goldstein, I.J.3
  • 38
    • 0024022763 scopus 로고
    • Structure and distribution of N-linked oligosaccharide chains on various domains of mouse tumor laminin
    • S. Fujiwara, H. Shinkai, R. Deutzmann, M. Paulsson, and R. Timpl Structure and distribution of N-linked oligosaccharide chains on various domains of mouse tumor laminin Biochem. J. 252 1988 453 461
    • (1988) Biochem. J. , vol.252 , pp. 453-461
    • Fujiwara, S.1    Shinkai, H.2    Deutzmann, R.3    Paulsson, M.4    Timpl, R.5
  • 39
    • 0033570105 scopus 로고    scopus 로고
    • Thermodynamic studies of saccharide binding to artocarpin, a B-cell mitogen, reveals the extended nature of its interaction with mannotriose [3,6-di-O-(alpha-d-mannopyranosyl)-d-mannose]
    • P.G. Rani, K. Bachhawat, S. Misquith, and A. Surolia Thermodynamic studies of saccharide binding to artocarpin, a B-cell mitogen, reveals the extended nature of its interaction with mannotriose [3,6-di-O-(alpha-d- mannopyranosyl)-d-mannose] J. Biol. Chem. 274 1999 29694 29698
    • (1999) J. Biol. Chem. , vol.274 , pp. 29694-29698
    • Rani, P.G.1    Bachhawat, K.2    Misquith, S.3    Surolia, A.4
  • 40
    • 0036295206 scopus 로고    scopus 로고
    • Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-d-mannose: Implications to the generation of carbohydrate specificity
    • J.V. Pratap, A.A. Jeyaprakash, P.G. Rani, K. Sekar, A. Surolia, and M. Vijayan Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-alpha-d-mannose: implications to the generation of carbohydrate specificity J. Mol. Biol. 317 2002 237 247
    • (2002) J. Mol. Biol. , vol.317 , pp. 237-247
    • Pratap, J.V.1    Jeyaprakash, A.A.2    Rani, P.G.3    Sekar, K.4    Surolia, A.5    Vijayan, M.6
  • 41
    • 1942489712 scopus 로고    scopus 로고
    • Structural basis for the carbohydrate specificities of artocarpin: Variation in the length of a loop as a strategy for generating ligand specificity
    • A.A. Jeyaprakash, A. Srivastav, A. Surolia, and M. Vijayan Structural basis for the carbohydrate specificities of artocarpin: variation in the length of a loop as a strategy for generating ligand specificity J. Mol. Biol. 338 2004 757 770
    • (2004) J. Mol. Biol. , vol.338 , pp. 757-770
    • Jeyaprakash, A.A.1    Srivastav, A.2    Surolia, A.3    Vijayan, M.4
  • 43
    • 0345269215 scopus 로고    scopus 로고
    • A structural basis for the difference in specificity between the two jacalin-related lectins from mulberry (Morus nigra) bark
    • P. Rouge, W.J. Peumans, A. Barre, and E.J. Damme A structural basis for the difference in specificity between the two jacalin-related lectins from mulberry (Morus nigra) bark Biochem. Biophys. Res. Commun. 304 2003 91 97
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 91-97
    • Rouge, P.1    Peumans, W.J.2    Barre, A.3    Damme, E.J.4
  • 44
    • 0019205258 scopus 로고
    • Neutrophil chemotaxis in response to surface-bound C5A
    • R.O. Webster, B. Zanolari, and P.M. Henson Neutrophil chemotaxis in response to surface-bound C5A Exp. Cell Res. 129 1980 55 62
    • (1980) Exp. Cell Res. , vol.129 , pp. 55-62
    • Webster, R.O.1    Zanolari, B.2    Henson, P.M.3
  • 46
    • 0026525276 scopus 로고
    • CD11/CD18-independent neutrophil adherence to laminin is mediated by the integrin VLA-6
    • J.F. Bohnsack CD11/CD18-independent neutrophil adherence to laminin is mediated by the integrin VLA-6 Blood 79 1992 1545 1552
    • (1992) Blood , vol.79 , pp. 1545-1552
    • Bohnsack, J.F.1
  • 47
    • 0034144191 scopus 로고    scopus 로고
    • Alpha 6 beta 1 integrin (VLA-6) mediates leukocyte tether and arrest on laminin under physiological shear flow
    • J. Kitayama, S. Ikeda, K. Kumagai, H. Saito, and H. Nagawa Alpha 6 beta 1 integrin (VLA-6) mediates leukocyte tether and arrest on laminin under physiological shear flow Cell. Immunol. 199 2000 97 103
    • (2000) Cell. Immunol. , vol.199 , pp. 97-103
    • Kitayama, J.1    Ikeda, S.2    Kumagai, K.3    Saito, H.4    Nagawa, H.5
  • 48
    • 0031850611 scopus 로고    scopus 로고
    • Maintenance of granulocyte numbers during acute peritonitis is defective in galectin-3-null mutant mice
    • C. Colnot, M.A. Ripoche, G. Milon, X. Montagutelli, P.R. Crocker, and F. Poirier Maintenance of granulocyte numbers during acute peritonitis is defective in galectin-3-null mutant mice Immunology 94 1998 290 296
    • (1998) Immunology , vol.94 , pp. 290-296
    • Colnot, C.1    Ripoche, M.A.2    Milon, G.3    Montagutelli, X.4    Crocker, P.R.5    Poirier, F.6
  • 49
    • 0028951736 scopus 로고
    • A human lectin, galectin-3 (epsilon-bp/Mac-2), stimulates superoxide production by neutrophils
    • A. Yamaoka, I. Kuwabara, L.G. Frigeri, and F.T. Liu A human lectin, galectin-3 (epsilon-bp/Mac-2), stimulates superoxide production by neutrophils J. Immunol. 154 1995 3479 3487
    • (1995) J. Immunol. , vol.154 , pp. 3479-3487
    • Yamaoka, A.1    Kuwabara, I.2    Frigeri, L.G.3    Liu, F.T.4
  • 50
    • 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 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, W.R.6
  • 51
    • 0020594320 scopus 로고
    • Dendritic cell and macrophage staining by monoclonal antibodies in tissue sections and epidermal sheets
    • T.J. Flotte, T.A. Springer, and G.J. Thorbecke Dendritic cell and macrophage staining by monoclonal antibodies in tissue sections and epidermal sheets Am. J. Pathol. 111 1983 112 124
    • (1983) Am. J. Pathol. , vol.111 , pp. 112-124
    • Flotte, T.J.1    Springer, T.A.2    Thorbecke, G.J.3
  • 52
    • 0034851982 scopus 로고    scopus 로고
    • Galectins as modulators of cell adhesion
    • R.C. Hughes Galectins as modulators of cell adhesion Biochimie 83 2001 667 676
    • (2001) Biochimie , vol.83 , pp. 667-676
    • Hughes, R.C.1
  • 53
    • 0031434585 scopus 로고    scopus 로고
    • Through and beyond the wall: Late steps in leukocyte transendothelial migration
    • E. Bianchi, J.R. Bender, F. Blasi, and R. Pardi Through and beyond the wall: late steps in leukocyte transendothelial migration Immunol. Today 18 1997 586 591
    • (1997) Immunol. Today , vol.18 , pp. 586-591
    • Bianchi, E.1    Bender, J.R.2    Blasi, F.3    Pardi, R.4
  • 54
    • 0037378123 scopus 로고    scopus 로고
    • Unique structural features that influence neutrophil emigration into the lung
    • A.R. Burns, C.W. Smith, and D.C. Walker Unique structural features that influence neutrophil emigration into the lung Physiol. Rev. 83 2003 309 336
    • (2003) Physiol. Rev. , vol.83 , pp. 309-336
    • Burns, A.R.1    Smith, C.W.2    Walker, D.C.3
  • 55
    • 0026694563 scopus 로고
    • Endothelial cell binding of NAP-1/IL-8: Role in neutrophil emigration
    • A. Rot Endothelial cell binding of NAP-1/IL-8: role in neutrophil emigration Immunol. Today 13 1992 291 294
    • (1992) Immunol. Today , vol.13 , pp. 291-294
    • Rot, A.1
  • 56
    • 0000280766 scopus 로고
    • Fibronectin and other cell interactive glycoproteins
    • E.D. Hay Plenum Press New York
    • K.M. Yamada Fibronectin and other cell interactive glycoproteins E.D. Hay Cell Biology Of Extracellular Matrix 1991 Plenum Press New York 111 146
    • (1991) Cell Biology of Extracellular Matrix , pp. 111-146
    • Yamada, K.M.1
  • 57
    • 0024335289 scopus 로고
    • Structures of asparagine-linked oligosaccharides of human placental fibronectin
    • M. Takamoto, T. Endo, M. Isemura, N. Kochibe, and A. Kobata Structures of asparagine-linked oligosaccharides of human placental fibronectin J. Biochem. 105 1989 742 750
    • (1989) J. Biochem. , vol.105 , pp. 742-750
    • Takamoto, M.1    Endo, T.2    Isemura, M.3    Kochibe, N.4    Kobata, A.5
  • 58
    • 0024346640 scopus 로고
    • Detection of bisected biantennary form in the asparagine-linked oligosaccharides of fibronectin isolated from human term amniotic fluid
    • M. Takamoto, T. Endo, M. Isemura, Y. Yamaguchi, K. Okamura, N. Kochibe, and A. Kobata Detection of bisected biantennary form in the asparagine-linked oligosaccharides of fibronectin isolated from human term amniotic fluid J. Biochem. 106 1989 228 235
    • (1989) J. Biochem. , vol.106 , pp. 228-235
    • Takamoto, M.1    Endo, T.2    Isemura, M.3    Yamaguchi, Y.4    Okamura, K.5    Kochibe, N.6    Kobata, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.