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Volumn 28, Issue 2, 2010, Pages 326-332

An immune responsive multidomain galectin from bay scallop Argopectens irradians

Author keywords

Argopectens irradians; Bacteria and yeast challenge; Galectin; mRNA expression; Quantitative real time PCR

Indexed keywords

ARGOPECTEN IRRADIANS; BACTERIA (MICROORGANISMS); INVERTEBRATA; LISTONELLA ANGUILLARUM; MICROCOCCUS LUTEUS; PECTINIDAE; PICHIA PASTORIS; VERTEBRATA;

EID: 74649085824     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2009.11.016     Document Type: Article
Times cited : (55)

References (43)
  • 3
    • 4744359093 scopus 로고    scopus 로고
    • Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates
    • Vasta G.R., Ahmed H., and Odom E.W. Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates. Curr Opin Struct Biol 14 5 (2004) 617-630
    • (2004) Curr Opin Struct Biol , vol.14 , Issue.5 , pp. 617-630
    • Vasta, G.R.1    Ahmed, H.2    Odom, E.W.3
  • 4
    • 0027169990 scopus 로고
    • The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution
    • Hirabayashi J., and Kasai K. The family of metazoan metal-independent beta-galactoside-binding lectins: structure, function and molecular evolution. Glycobiology 3 4 (1993) 297-304
    • (1993) Glycobiology , vol.3 , Issue.4 , pp. 297-304
    • Hirabayashi, J.1    Kasai, K.2
  • 5
    • 2542591692 scopus 로고    scopus 로고
    • Discovery and characterization of an epithelial-specific galectin in the endometrium that forms crystals in the trophectoderm
    • Gray C.A., Adelson D.L., Bazer F.W., Burghardt R.C., Meeusen E.N., and Spencer T.E. Discovery and characterization of an epithelial-specific galectin in the endometrium that forms crystals in the trophectoderm. Proc Natl Acad Sci U S A 101 21 (2004) 7982-7987
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.21 , pp. 7982-7987
    • Gray, C.A.1    Adelson, D.L.2    Bazer, F.W.3    Burghardt, R.C.4    Meeusen, E.N.5    Spencer, T.E.6
  • 6
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer C.F., Miceli M.C., and Baum L.G. Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr Opin Struct Biol 12 5 (2002) 616-623
    • (2002) Curr Opin Struct Biol , vol.12 , Issue.5 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 7
    • 33947161979 scopus 로고    scopus 로고
    • Dissecting the pathophysiologic role of endogenous lectins: glycan-binding proteins with cytokine-like activity?
    • Toscano M.A., Ilarregui J.M., Bianco G.A., Campagna L., Croci D.O., Salatino M., et al. Dissecting the pathophysiologic role of endogenous lectins: glycan-binding proteins with cytokine-like activity?. Cytokine Growth Factor Rev 18 1-2 (2007) 57-71
    • (2007) Cytokine Growth Factor Rev , vol.18 , Issue.1-2 , pp. 57-71
    • Toscano, M.A.1    Ilarregui, J.M.2    Bianco, G.A.3    Campagna, L.4    Croci, D.O.5    Salatino, M.6
  • 8
    • 0030049078 scopus 로고    scopus 로고
    • The animal lectin galectin-3 interacts with bacterial lipopolysaccharides via two independent sites
    • Mey A., Leffler H., Hmama Z., Normier G., and Revillard J.P. The animal lectin galectin-3 interacts with bacterial lipopolysaccharides via two independent sites. J Immunol 156 4 (1996) 1572-1577
    • (1996) J Immunol , vol.156 , Issue.4 , pp. 1572-1577
    • Mey, A.1    Leffler, H.2    Hmama, Z.3    Normier, G.4    Revillard, J.P.5
  • 9
    • 0034737701 scopus 로고    scopus 로고
    • Novel mechanism that Trypanosoma cruzi uses to adhere to the extracellular matrix mediated by human galectin-3
    • Moody T.N., Ochieng J., and Villalta F. Novel mechanism that Trypanosoma cruzi uses to adhere to the extracellular matrix mediated by human galectin-3. FEBS Lett 470 3 (2000) 305-308
    • (2000) FEBS Lett , vol.470 , Issue.3 , pp. 305-308
    • Moody, T.N.1    Ochieng, J.2    Villalta, F.3
  • 10
    • 0038605468 scopus 로고    scopus 로고
    • Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells
    • Pelletier I., Hashidate T., Urashima T., Nishi N., Nakamura T., Futai M., et al. Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells. J Biol Chem 278 25 (2003) 22223-22230
    • (2003) J Biol Chem , vol.278 , Issue.25 , pp. 22223-22230
    • Pelletier, I.1    Hashidate, T.2    Urashima, T.3    Nishi, N.4    Nakamura, T.5    Futai, M.6
  • 11
    • 15444380346 scopus 로고    scopus 로고
    • Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells
    • Ouellet M., Mercier S., Pelletier I., Bounou S., Roy J., Hirabayashi J., et al. Galectin-1 acts as a soluble host factor that promotes HIV-1 infectivity through stabilization of virus attachment to host cells. J Immunol 174 7 (2005) 4120-4126
    • (2005) J Immunol , vol.174 , Issue.7 , pp. 4120-4126
    • Ouellet, M.1    Mercier, S.2    Pelletier, I.3    Bounou, S.4    Roy, J.5    Hirabayashi, J.6
  • 12
    • 20444419772 scopus 로고    scopus 로고
    • Galectins as immunoregulators during infectious processes: from microbial invasion to the resolution of the disease
    • Rabinovich G.A., and Gruppi A. Galectins as immunoregulators during infectious processes: from microbial invasion to the resolution of the disease. Parasite Immunol 27 4 (2005) 103-114
    • (2005) Parasite Immunol , vol.27 , Issue.4 , pp. 103-114
    • Rabinovich, G.A.1    Gruppi, A.2
  • 13
  • 14
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway Jr. C.A. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol 54 Pt 1 (1989) 1-13
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PART 1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 15
    • 0033975869 scopus 로고    scopus 로고
    • Innate immune recognition: mechanisms and pathways
    • Medzhitov R., and Janeway Jr. C. Innate immune recognition: mechanisms and pathways. Immunol Rev 173 (2000) 89-97
    • (2000) Immunol Rev , vol.173 , pp. 89-97
    • Medzhitov, R.1    Janeway Jr., C.2
  • 17
    • 0030831258 scopus 로고    scopus 로고
    • A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection
    • Adema C.M., Hertel L.A., Miller R.D., and Loker E.S. A family of fibrinogen-related proteins that precipitates parasite-derived molecules is produced by an invertebrate after infection. Proc Natl Acad Sci U S A 94 16 (1997) 8691-8696
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.16 , pp. 8691-8696
    • Adema, C.M.1    Hertel, L.A.2    Miller, R.D.3    Loker, E.S.4
  • 18
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • Vasta G.R. Roles of galectins in infection. Nat Rev Microbiol 7 6 (2009) 424-438
    • (2009) Nat Rev Microbiol , vol.7 , Issue.6 , pp. 424-438
    • Vasta, G.R.1
  • 19
    • 35548934271 scopus 로고    scopus 로고
    • A galectin of unique domain organization from hemocytes of the Eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus
    • Tasumi S., and Vasta G.R. A galectin of unique domain organization from hemocytes of the Eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus. J Immunol 179 5 (2007) 3086-3098
    • (2007) J Immunol , vol.179 , Issue.5 , pp. 3086-3098
    • Tasumi, S.1    Vasta, G.R.2
  • 20
    • 39749172949 scopus 로고    scopus 로고
    • Molecular and functional characterization of a tandem-repeat galectin from the freshwater snail Biomphalaria glabrata, intermediate host of the human blood fluke Schistosoma mansoni
    • Yoshino T.P., Dinguirard N., Kunert J., and Hokke C.H. Molecular and functional characterization of a tandem-repeat galectin from the freshwater snail Biomphalaria glabrata, intermediate host of the human blood fluke Schistosoma mansoni. Gene 411 1-2 (2008) 46-58
    • (2008) Gene , vol.411 , Issue.1-2 , pp. 46-58
    • Yoshino, T.P.1    Dinguirard, N.2    Kunert, J.3    Hokke, C.H.4
  • 21
    • 46549085873 scopus 로고    scopus 로고
    • Noble tandem-repeat galectin of Manila clam Ruditapes philippinarum is induced upon infection with the protozoan parasite Perkinsus olseni
    • Kim J.Y., Kim Y.M., Cho S.K., Choi K.S., and Cho M. Noble tandem-repeat galectin of Manila clam Ruditapes philippinarum is induced upon infection with the protozoan parasite Perkinsus olseni. Dev Comp Immunol 32 (2008) 1131-1141
    • (2008) Dev Comp Immunol , vol.32 , pp. 1131-1141
    • Kim, J.Y.1    Kim, Y.M.2    Cho, S.K.3    Choi, K.S.4    Cho, M.5
  • 22
    • 33646476745 scopus 로고    scopus 로고
    • Development of expressed sequence tags from the bay scallop, Argopecten irradians irradians
    • Song L., Xu W., Li C., Li H., Wu L., Xiang J., et al. Development of expressed sequence tags from the bay scallop, Argopecten irradians irradians. Mar Biotechnol (NY) 8 (2006) 161-169
    • (2006) Mar Biotechnol (NY) , vol.8 , pp. 161-169
    • Song, L.1    Xu, W.2    Li, C.3    Li, H.4    Wu, L.5    Xiang, J.6
  • 23
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25 24 (1997) 4876-4882
    • (1997) Nucleic Acids Res , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 24
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., and Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4 4 (1987) 406-425
    • (1987) Mol Biol Evol , vol.4 , Issue.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 25
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 5 2 (2004) 150-163
    • (2004) Brief Bioinform , vol.5 , Issue.2 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 26
    • 50149106793 scopus 로고    scopus 로고
    • A novel C1q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity
    • Zhang H., Song L., Li C., Zhao J., Wang H., Qiu L., et al. A novel C1q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity. Fish Shellfish Immunol 25 (2008) 281-289
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 281-289
    • Zhang, H.1    Song, L.2    Li, C.3    Zhao, J.4    Wang, H.5    Qiu, L.6
  • 27
    • 33747829917 scopus 로고    scopus 로고
    • Molecular cloning, expression of a big defensin gene from bay scallop Argopecten irradians and the antimicrobial activity of its recombinant protein
    • Zhao J., Song L., Li C., Ni D., Wu L., Zhu L., et al. Molecular cloning, expression of a big defensin gene from bay scallop Argopecten irradians and the antimicrobial activity of its recombinant protein. Mol Immunol 44 4 (2007) 360-368
    • (2007) Mol Immunol , vol.44 , Issue.4 , pp. 360-368
    • Zhao, J.1    Song, L.2    Li, C.3    Ni, D.4    Wu, L.5    Zhu, L.6
  • 28
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25 4 (2001) 402-408
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 29
    • 0028676128 scopus 로고
    • Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides
    • Bourne Y., Bolgiano B., Liao D.I., Strecker G., Cantau P., Herzberg O., et al. Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides. Nat Struct Biol 1 12 (1994) 863-870
    • (1994) Nat Struct Biol , vol.1 , Issue.12 , pp. 863-870
    • Bourne, Y.1    Bolgiano, B.2    Liao, D.I.3    Strecker, G.4    Cantau, P.5    Herzberg, O.6
  • 30
    • 0027965708 scopus 로고
    • Structure and function of a large family of animal lectins
    • Barondes S.H., Cooper D.N., Gitt M.A., and Galectins L.H. Structure and function of a large family of animal lectins. J Biol Chem 269 33 (1994) 20807-20810
    • (1994) J Biol Chem , vol.269 , Issue.33 , pp. 20807-20810
    • Barondes, S.H.1    Cooper, D.N.2    Gitt, M.A.3    Galectins, L.H.4
  • 31
    • 0027958144 scopus 로고
    • Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein
    • Liao D.I., Kapadia G., Ahmed H., Vasta G.R., and Herzberg O. Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein. Proc Natl Acad Sci U S A 91 4 (1994) 1428-1432
    • (1994) Proc Natl Acad Sci U S A , vol.91 , Issue.4 , pp. 1428-1432
    • Liao, D.I.1    Kapadia, G.2    Ahmed, H.3    Vasta, G.R.4    Herzberg, O.5
  • 32
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: finding themes in complexity
    • Cooper D.N. Galectinomics: finding themes in complexity. Biochim Biophys Acta 1572 2-3 (2002) 209-231
    • (2002) Biochim Biophys Acta , vol.1572 , Issue.2-3 , pp. 209-231
    • Cooper, D.N.1
  • 33
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • Nickel W. The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur J Biochem 270 10 (2003) 2109-2119
    • (2003) Eur J Biochem , vol.270 , Issue.10 , pp. 2109-2119
    • Nickel, W.1
  • 34
  • 35
    • 0028229493 scopus 로고
    • Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism
    • Mahanthappa N.K., Cooper D.N., Barondes S.H., and Schwarting G.A. Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism. Development 120 6 (1994) 1373-1384
    • (1994) Development , vol.120 , Issue.6 , pp. 1373-1384
    • Mahanthappa, N.K.1    Cooper, D.N.2    Barondes, S.H.3    Schwarting, G.A.4
  • 36
    • 0037136408 scopus 로고    scopus 로고
    • Role of galectins in inflammatory and immunomodulatory processes
    • Rabinovich G.A., Rubinstein N., and Toscano M.A. Role of galectins in inflammatory and immunomodulatory processes. Biochim Biophys Acta 1572 2-3 (2002) 274-284
    • (2002) Biochim Biophys Acta , vol.1572 , Issue.2-3 , pp. 274-284
    • Rabinovich, G.A.1    Rubinstein, N.2    Toscano, M.A.3
  • 37
    • 0036798862 scopus 로고    scopus 로고
    • Ah, sweet mystery of death! Galectins and control of cell fate
    • Hernandez J.D., and Baum L.G. Ah, sweet mystery of death! Galectins and control of cell fate. Glycobiology 12 10 (2002) 127R-136R
    • (2002) Glycobiology , vol.12 , Issue.10
    • Hernandez, J.D.1    Baum, L.G.2
  • 38
    • 0025201026 scopus 로고
    • Evidence for the role of 34-kDa galactoside-binding lectin in transformation and metastasis
    • Raz A., Zhu D.G., Hogan V., Shah N., Raz T., Karkash R., et al. Evidence for the role of 34-kDa galactoside-binding lectin in transformation and metastasis. Int J Cancer 46 5 (1990) 871-877
    • (1990) Int J Cancer , vol.46 , Issue.5 , pp. 871-877
    • Raz, A.1    Zhu, D.G.2    Hogan, V.3    Shah, N.4    Raz, T.5    Karkash, R.6
  • 39
    • 0036790940 scopus 로고    scopus 로고
    • Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering
    • Gauthier L., Rossi B., Roux F., Termine E., and Schiff C. Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering. Proc Natl Acad Sci U S A 99 20 (2002) 13014-13019
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.20 , pp. 13014-13019
    • Gauthier, L.1    Rossi, B.2    Roux, F.3    Termine, E.4    Schiff, C.5
  • 40
    • 3242781553 scopus 로고    scopus 로고
    • LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition
    • van den Berg T.K., Honing H., Franke N., van Remoortere A., Schiphorst W.E., Liu F.T., et al. LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition. J Immunol 173 3 (2004) 1902-1907
    • (2004) J Immunol , vol.173 , Issue.3 , pp. 1902-1907
    • van den Berg, T.K.1    Honing, H.2    Franke, N.3    van Remoortere, A.4    Schiphorst, W.E.5    Liu, F.T.6
  • 41
    • 0037124095 scopus 로고    scopus 로고
    • Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope
    • Pelletier I., and Sato S. Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope. J Biol Chem 277 20 (2002) 17663-17670
    • (2002) J Biol Chem , vol.277 , Issue.20 , pp. 17663-17670
    • Pelletier, I.1    Sato, S.2
  • 42
    • 34447295924 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of galectin from amphioxus: primitive galectin of chordates participated in the infection processes
    • Yu Y., Yuan S., Yu Y., Huang H., Feng K., Pan M., et al. Molecular and biochemical characterization of galectin from amphioxus: primitive galectin of chordates participated in the infection processes. Glycobiology 17 7 (2007) 774-783
    • (2007) Glycobiology , vol.17 , Issue.7 , pp. 774-783
    • Yu, Y.1    Yuan, S.2    Yu, Y.3    Huang, H.4    Feng, K.5    Pan, M.6
  • 43
    • 0037687733 scopus 로고    scopus 로고
    • Cell adhesion-related gene expression by Helicobacter pylori in gastric epithelial AGS cells
    • Lim J.W., Kim H., and Kim K.H. Cell adhesion-related gene expression by Helicobacter pylori in gastric epithelial AGS cells. Int J Biochem Cell Biol 35 8 (2003) 1284-1296
    • (2003) Int J Biochem Cell Biol , vol.35 , Issue.8 , pp. 1284-1296
    • Lim, J.W.1    Kim, H.2    Kim, K.H.3


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