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Volumn 27, Issue 3, 2009, Pages 478-485

Identification of l-fucose-binding proteins from the Nile tilapia (Oreochromis niloticus L.) serum

Author keywords

Affinity chromatography; Fucolectin; Fucose binding protein; Nile tilapia serum

Indexed keywords

AEROMONAS HYDROPHILA; ARMORACIA RUSTICANA; ENTEROCOCCUS FAECALIS; OREOCHROMIS NILOTICUS; TILAPIA;

EID: 68949141663     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2009.06.012     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 0038348638 scopus 로고    scopus 로고
    • Role of the mannose-binding lectin in innate immunity
    • Ezekowitz R.A. Role of the mannose-binding lectin in innate immunity. J Infect Dis 187 Suppl. 2 (2003) S335-S339
    • (2003) J Infect Dis , vol.187 , Issue.SUPPL. 2
    • Ezekowitz, R.A.1
  • 2
    • 22844435410 scopus 로고    scopus 로고
    • Innate immunity of fish (overview)
    • Magnadottir B. Innate immunity of fish (overview). Fish Shellfish Immunol 20 (2006) 137-151
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 137-151
    • Magnadottir, B.1
  • 3
    • 0024553735 scopus 로고
    • The human mannose-binding protein functions as an opsonin
    • Kuhlman M., Joiner K., and Ezekowitz R.A. The human mannose-binding protein functions as an opsonin. J Exp Med 169 (1989) 1733-1745
    • (1989) J Exp Med , vol.169 , pp. 1733-1745
    • Kuhlman, M.1    Joiner, K.2    Ezekowitz, R.A.3
  • 5
    • 0028006866 scopus 로고
    • Complement-dependent cytotoxic activity of serum mannan-binding protein towards mammalian cells with surface-exposed high-mannose type glycans
    • Ohta M., and Kawasaki T. Complement-dependent cytotoxic activity of serum mannan-binding protein towards mammalian cells with surface-exposed high-mannose type glycans. Glycoconjug J 11 (1994) 304-308
    • (1994) Glycoconjug J , vol.11 , pp. 304-308
    • Ohta, M.1    Kawasaki, T.2
  • 6
    • 0021763384 scopus 로고
    • Physicochemical properties and N-terminal sequence of eel lectin
    • Kelly C. Physicochemical properties and N-terminal sequence of eel lectin. Biochem J 220 (1984) 221-226
    • (1984) Biochem J , vol.220 , pp. 221-226
    • Kelly, C.1
  • 7
    • 0034693055 scopus 로고    scopus 로고
    • Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins
    • Honda S., Kashiwagi M., Miyamoto K., Takei Y., and Hirose S. Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins. J Biol Chem 275 (2000) 33151-33157
    • (2000) J Biol Chem , vol.275 , pp. 33151-33157
    • Honda, S.1    Kashiwagi, M.2    Miyamoto, K.3    Takei, Y.4    Hirose, S.5
  • 8
    • 0027982478 scopus 로고
    • A new mannan-binding lectin from the serum of the eel (Anguilla-anguilla l.) - isolation, characterization and comparison with the fucose-specific serum lectin
    • Gercken J., and Renwrantz L. A new mannan-binding lectin from the serum of the eel (Anguilla-anguilla l.) - isolation, characterization and comparison with the fucose-specific serum lectin. Comp Biochem Physiol B-Biochem & Mol Biol 108 (1994) 449-461
    • (1994) Comp Biochem Physiol B-Biochem & Mol Biol , vol.108 , pp. 449-461
    • Gercken, J.1    Renwrantz, L.2
  • 9
    • 33644981902 scopus 로고    scopus 로고
    • Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis)
    • Odom E., and Vasta G.R. Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis). J Biol Chem 281 (2006) 1698-1713
    • (2006) J Biol Chem , vol.281 , pp. 1698-1713
    • Odom, E.1    Vasta, G.R.2
  • 10
    • 33845427599 scopus 로고    scopus 로고
    • Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum
    • Cammarata M., Benenati G., Odom E.W., Salerno G., Vizzini A., Vasta G.R., et al. Isolation and characterization of a fish F-type lectin from gilt head bream (Sparus aurata) serum. Biochim Biophys Acta 1770 (2007) 150-155
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 150-155
    • Cammarata, M.1    Benenati, G.2    Odom, E.W.3    Salerno, G.4    Vizzini, A.5    Vasta, G.R.6
  • 12
    • 0034239019 scopus 로고    scopus 로고
    • Isolation and characterisation of a serum lectin from blue gourami, Trichogaster trichopterus (Pallus)
    • Fock W.L., Chen C.L., Lam T.J., and Sin Y.M. Isolation and characterisation of a serum lectin from blue gourami, Trichogaster trichopterus (Pallus). Fish Shellfish Immunol 10 (2000) 489-504
    • (2000) Fish Shellfish Immunol , vol.10 , pp. 489-504
    • Fock, W.L.1    Chen, C.L.2    Lam, T.J.3    Sin, Y.M.4
  • 14
    • 0003159641 scopus 로고
    • Synthetic ligands for lectins
    • Gabius H.-J., and Gabius S. (Eds), Springer-Verlag, Berlin
    • Lee R.T., and Lee Y.C. Synthetic ligands for lectins. In: Gabius H.-J., and Gabius S. (Eds). Lectins and glycobiology (1993), Springer-Verlag, Berlin 9-22
    • (1993) Lectins and glycobiology , pp. 9-22
    • Lee, R.T.1    Lee, Y.C.2
  • 15
    • 0036312626 scopus 로고    scopus 로고
    • A novel fucose recognition fold involved in innate immunity
    • Bianchet M.A., Odom E.W., Vasta G.R., and Amzel L.M. A novel fucose recognition fold involved in innate immunity. Nat Struct Biol 9 (2002) 628-634
    • (2002) Nat Struct Biol , vol.9 , pp. 628-634
    • Bianchet, M.A.1    Odom, E.W.2    Vasta, G.R.3    Amzel, L.M.4
  • 16
    • 0023087990 scopus 로고
    • Lectin-binding characteristics of related high- and low-metastatic rat mammary adenocarcinoma cell lines
    • Badenoch-Jones P., Claudianos C., and Ramshaw I.A. Lectin-binding characteristics of related high- and low-metastatic rat mammary adenocarcinoma cell lines. Invasion Metastasis 7 (1987) 284-296
    • (1987) Invasion Metastasis , vol.7 , pp. 284-296
    • Badenoch-Jones, P.1    Claudianos, C.2    Ramshaw, I.A.3
  • 17
    • 18244407072 scopus 로고    scopus 로고
    • Fucolectins in diagnostic and neoplasm investigation
    • Praizel O., Iamskov I.A., and Evstigneeva R.P. Fucolectins in diagnostic and neoplasm investigation. Biomed Khim 50 (2004) 420-435
    • (2004) Biomed Khim , vol.50 , pp. 420-435
    • Praizel, O.1    Iamskov, I.A.2    Evstigneeva, R.P.3
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0024348923 scopus 로고
    • Immobilization of proteins on oxidized crosslinked sepharose preparations by reductive amination
    • Stults N.L., Asta L.M., and Lee Y.C. Immobilization of proteins on oxidized crosslinked sepharose preparations by reductive amination. Anal Biochem 180 (1989) 114-119
    • (1989) Anal Biochem , vol.180 , pp. 114-119
    • Stults, N.L.1    Asta, L.M.2    Lee, Y.C.3
  • 20
    • 0031568262 scopus 로고    scopus 로고
    • 3-(4-carboxybenzoyl)quinoline-2-carboxaldehyde, a reagent with broad dynamic range for the assay of proteins and lipoproteins in solution
    • You W., Haugland R., Ryan D., and Haugland R. 3-(4-carboxybenzoyl)quinoline-2-carboxaldehyde, a reagent with broad dynamic range for the assay of proteins and lipoproteins in solution. Anal Biochem 244 (1997) 277-282
    • (1997) Anal Biochem , vol.244 , pp. 277-282
    • You, W.1    Haugland, R.2    Ryan, D.3    Haugland, R.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0029075044 scopus 로고
    • A silver stain protocol for proteins yielding high resolution and transparent background in sodium dodecyl sulfate-polyacrylamide gels
    • Swain M., and Ross N.W. A silver stain protocol for proteins yielding high resolution and transparent background in sodium dodecyl sulfate-polyacrylamide gels. Electrophoresis 16 (1995) 948-951
    • (1995) Electrophoresis , vol.16 , pp. 948-951
    • Swain, M.1    Ross, N.W.2
  • 23
    • 0003254592 scopus 로고
    • Electrophoretic analysis methods
    • Harris E.L.V., and Angal S. (Eds), Oxford University Press, New York
    • Dunn M.J. Electrophoretic analysis methods. In: Harris E.L.V., and Angal S. (Eds). Protein purification methods (1989), Oxford University Press, New York 18-37
    • (1989) Protein purification methods , pp. 18-37
    • Dunn, M.J.1
  • 25
    • 0003162226 scopus 로고    scopus 로고
    • The nonspecific immune system: humoral defense
    • Iwama G., and Nakanishi T. (Eds), Academic Press, San Diego, CA
    • Yano T. The nonspecific immune system: humoral defense. In: Iwama G., and Nakanishi T. (Eds). The fish immune system (1996), Academic Press, San Diego, CA 106-140
    • (1996) The fish immune system , pp. 106-140
    • Yano, T.1
  • 26
    • 0017927524 scopus 로고
    • Studies on lectins. XXXVI. Properties of some lectins prepared by affinity chromatography on O-glycosyl polyacrylamide gels
    • Horejsi V., and Kocourek J. Studies on lectins. XXXVI. Properties of some lectins prepared by affinity chromatography on O-glycosyl polyacrylamide gels. Biochim Biophys Acta 538 (1978) 299-315
    • (1978) Biochim Biophys Acta , vol.538 , pp. 299-315
    • Horejsi, V.1    Kocourek, J.2
  • 27
    • 0025250323 scopus 로고
    • Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine
    • Wellner D., Panneerselvam C., and Horecker B.L. Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine. Proc Natl Acad Sci U S A 87 (1990) 1947-1949
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 1947-1949
    • Wellner, D.1    Panneerselvam, C.2    Horecker, B.L.3
  • 28
    • 0033025199 scopus 로고    scopus 로고
    • Changes in serum concentration of a serum amyloid P-like pentraxin in Atlantic salmon, Salmo salar l., during infection and inflammation
    • Lund V., and Olafsen J.A. Changes in serum concentration of a serum amyloid P-like pentraxin in Atlantic salmon, Salmo salar l., during infection and inflammation. Dev Comp Immunol 23 (1999) 61-70
    • (1999) Dev Comp Immunol , vol.23 , pp. 61-70
    • Lund, V.1    Olafsen, J.A.2
  • 30
  • 31
    • 60649115620 scopus 로고    scopus 로고
    • Characterization of IgM of Indian major carps and their cross-reactivity with anti-fish IgM antibodies
    • Bag M.R., Makesh M., Rajendran K.V., and Mukherjee S.C. Characterization of IgM of Indian major carps and their cross-reactivity with anti-fish IgM antibodies. Fish Shellfish Immunol 26 (2009) 275-278
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 275-278
    • Bag, M.R.1    Makesh, M.2    Rajendran, K.V.3    Mukherjee, S.C.4
  • 32
    • 0028132023 scopus 로고
    • Physical biochemical properties of IgM from a teleost fish
    • Mochida K., Lou Y.H., Hara A., and Yamauchi K. Physical biochemical properties of IgM from a teleost fish. Immunology 83 (1994) 675-680
    • (1994) Immunology , vol.83 , pp. 675-680
    • Mochida, K.1    Lou, Y.H.2    Hara, A.3    Yamauchi, K.4
  • 33
    • 0035239218 scopus 로고    scopus 로고
    • Immune responses of Nile tilapia (Oreochromis niloticus L.) clones: I. Non-specific responses
    • Sarder M.R., Thompson K.D., Penman D.J., and McAndrew B.J. Immune responses of Nile tilapia (Oreochromis niloticus L.) clones: I. Non-specific responses. Dev Comp Immunol 25 (2001) 37-46
    • (2001) Dev Comp Immunol , vol.25 , pp. 37-46
    • Sarder, M.R.1    Thompson, K.D.2    Penman, D.J.3    McAndrew, B.J.4
  • 34
    • 0034216271 scopus 로고    scopus 로고
    • In vivo activation of tilapia nonspecific cytotoxic cells by Streptococcus iniae and amplification with apoptosis regulatory factor(s)
    • Evans D.L., Taylor S.L., Leary III J.H., Bishop G.R., Eldar A., and Jaso-Friedmann L. In vivo activation of tilapia nonspecific cytotoxic cells by Streptococcus iniae and amplification with apoptosis regulatory factor(s). Fish Shellfish Immunol 10 (2000) 419-434
    • (2000) Fish Shellfish Immunol , vol.10 , pp. 419-434
    • Evans, D.L.1    Taylor, S.L.2    Leary III, J.H.3    Bishop, G.R.4    Eldar, A.5    Jaso-Friedmann, L.6
  • 35
    • 23644460858 scopus 로고    scopus 로고
    • Molecular characterization of a widespread, pathogenic, and antibiotic resistance-receptive Enterococcus faecalis lineage and dissemination of its putative pathogenicity island
    • Nallapareddy S.R., Wenxiang H., Weinstock G.M., and Murray B.E. Molecular characterization of a widespread, pathogenic, and antibiotic resistance-receptive Enterococcus faecalis lineage and dissemination of its putative pathogenicity island. J Bacteriol 187 (2005) 5709-5718
    • (2005) J Bacteriol , vol.187 , pp. 5709-5718
    • Nallapareddy, S.R.1    Wenxiang, H.2    Weinstock, G.M.3    Murray, B.E.4
  • 36
    • 0003232458 scopus 로고    scopus 로고
    • Interactions of microbial glycoconjugates with collectins
    • Doyle (Ed), Kluwer Academic/Plenum Publishers, New York [p]
    • Ofek I., and Crouch E.C. Interactions of microbial glycoconjugates with collectins. In: Doyle (Ed). Glycomicrobiology (2000), Kluwer Academic/Plenum Publishers, New York [p]
    • (2000) Glycomicrobiology
    • Ofek, I.1    Crouch, E.C.2
  • 37
    • 0026311258 scopus 로고
    • Serum dependent expression of Enterococcus faecalis adhesins involved in the colonization of heart cells
    • Guzman C.A., Pruzzo C., Plate M., Guardati M.C., and Calegari L. Serum dependent expression of Enterococcus faecalis adhesins involved in the colonization of heart cells. Microb Pathog 11 (1991) 399-409
    • (1991) Microb Pathog , vol.11 , pp. 399-409
    • Guzman, C.A.1    Pruzzo, C.2    Plate, M.3    Guardati, M.C.4    Calegari, L.5
  • 38
    • 0342529369 scopus 로고
    • Isolation of plant lectins
    • Gabius H.-J., and Gabius S. (Eds), Springer-Verlag, Berlin
    • Rudiger H. Isolation of plant lectins. In: Gabius H.-J., and Gabius S. (Eds). Lectins and glycobiology (1993), Springer-Verlag, Berlin 31-46
    • (1993) Lectins and glycobiology , pp. 31-46
    • Rudiger, H.1
  • 40
    • 2942648240 scopus 로고    scopus 로고
    • Lectinochemical studies on the affinity of Anguilla anguilla agglutinin for mammalian glycotopes
    • Wu A.M., Wu J.H., Singh T., Liu J.H., and Herp A. Lectinochemical studies on the affinity of Anguilla anguilla agglutinin for mammalian glycotopes. Life Sci 75 (2004) 1085-1103
    • (2004) Life Sci , vol.75 , pp. 1085-1103
    • Wu, A.M.1    Wu, J.H.2    Singh, T.3    Liu, J.H.4    Herp, A.5
  • 41
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis W.I., Drickamer K., and Hendrickson W.A. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360 (1992) 127-134
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 42
    • 0035890468 scopus 로고    scopus 로고
    • Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica)
    • Mistry A.C., Honda S., and Hirose S. Structure, properties and enhanced expression of galactose-binding C-type lectins in mucous cells of gills from freshwater Japanese eels (Anguilla japonica). Biochem J 360 (2001) 107-115
    • (2001) Biochem J , vol.360 , pp. 107-115
    • Mistry, A.C.1    Honda, S.2    Hirose, S.3
  • 43
    • 0001044156 scopus 로고    scopus 로고
    • The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
    • Ewart K.V., Li Z., Yang D.S., Fletcher G.L., and Hew C.L. The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins. Biochemistry 37 (1998) 4080-4085
    • (1998) Biochemistry , vol.37 , pp. 4080-4085
    • Ewart, K.V.1    Li, Z.2    Yang, D.S.3    Fletcher, G.L.4    Hew, C.L.5
  • 44
    • 0037424801 scopus 로고    scopus 로고
    • Cloning and characterization of the Atlantic salmon serum lectin, a long-form C-type lectin expressed in kidney
    • Richards R.C., Hudson D.M., Thibault P., and Ewart K.V. Cloning and characterization of the Atlantic salmon serum lectin, a long-form C-type lectin expressed in kidney. Biochim Biophys Acta 1621 (2003) 110-115
    • (2003) Biochim Biophys Acta , vol.1621 , pp. 110-115
    • Richards, R.C.1    Hudson, D.M.2    Thibault, P.3    Ewart, K.V.4


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