메뉴 건너뛰기




Volumn 1725, Issue 2, 2005, Pages 160-173

Purification, characterization, cDNA cloning, and expression of asialofetuin-binding C-type lectin from eggs of shishamo smelt (Osmerus [Spirinchus] lanceolatus)

Author keywords

Asialofetuin; C type lectin; Calcium independent; EPN sequence; Fish egg; Heterodimer

Indexed keywords

ASIALOFETUIN; BUFFER; CALCIUM ION; COLLECTIN; COMPLEMENTARY DNA; DIMER; GALACTOSE; GLUCOSE; HISTIDINE; ISOPROTEIN; LACTOSE; LECTIN; MANNOSE; RECOMBINANT PROTEIN; RHAMNOSE; SEPHAROSE;

EID: 24344485120     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.07.009     Document Type: Article
Times cited : (55)

References (50)
  • 1
    • 0002830651 scopus 로고
    • Egg lectins of invertebrates and lower vertebrates: Properties and biological function
    • A. Krajhanzl Egg lectins of invertebrates and lower vertebrates: properties and biological function Adv. Lectin Res. 3 1990 83 131
    • (1990) Adv. Lectin Res. , vol.3 , pp. 83-131
    • Krajhanzl, A.1
  • 5
    • 0032563094 scopus 로고    scopus 로고
    • Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily
    • H. Tateno, A. Saneyoshi, T. Ogawa, K. Muramoto, H. Kamiya, and M. Saneyoshi Isolation and characterization of rhamnose-binding lectins from eggs of steelhead trout (Oncorhynchus mykiss) homologous to low density lipoprotein receptor superfamily J. Biol. Chem. 273 1998 19190 19197
    • (1998) J. Biol. Chem. , vol.273 , pp. 19190-19197
    • Tateno, H.1    Saneyoshi, A.2    Ogawa, T.3    Muramoto, K.4    Kamiya, H.5    Saneyoshi, M.6
  • 6
    • 0036616919 scopus 로고    scopus 로고
    • Distribution and molecular evolution of rhamnose-binding lectins in Salmonidae: Isolation and characterization of two lectins from white-spotted Charr (Salvelinus leucomaenis) eggs
    • H. Tateno, T. Ogawa, K. Muramoto, H. Kamiya, and M. Saneyoshi Distribution and molecular evolution of rhamnose-binding lectins in Salmonidae: isolation and characterization of two lectins from white-spotted Charr (Salvelinus leucomaenis) eggs Biosci. Biotechnol. Biochem. 66 2002 1356 1365
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1356-1365
    • Tateno, H.1    Ogawa, T.2    Muramoto, K.3    Kamiya, H.4    Saneyoshi, M.5
  • 7
    • 0025907124 scopus 로고
    • Amino acid sequence and molecular characterization of a d-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs
    • Y. Ozeki, T. Matsui, M. Suzuki, and K. Titani Amino acid sequence and molecular characterization of a d-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs Biochemistry 30 1991 2391 2394
    • (1991) Biochemistry , vol.30 , pp. 2391-2394
    • Ozeki, Y.1    Matsui, T.2    Suzuki, M.3    Titani, K.4
  • 8
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • P.H. Weigel, and J.H. Yik Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors Biochim. Biophys. Acta 1572 2002 341 363
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.2
  • 9
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity
    • R.B. Dodd, and K. Drickamer Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity Glycobiology 11 2001 71R 79R
    • (2001) Glycobiology , vol.11
    • Dodd, R.B.1    Drickamer, K.2
  • 10
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: A historical introduction and overview
    • D.C. Kilpatrick Animal lectins: a historical introduction and overview Biochim. Biophys. Acta 1572 2002 187 197
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.C.1
  • 11
    • 0033428909 scopus 로고    scopus 로고
    • C-type lectin-like domains in Caenorhabditis elegans: Predictions from the complete genome sequence
    • K. Drickamer, and R.B. Dodd C-type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence Glycobiology 9 1999 1357 1369
    • (1999) Glycobiology , vol.9 , pp. 1357-1369
    • Drickamer, K.1    Dodd, R.B.2
  • 13
    • 0037178884 scopus 로고    scopus 로고
    • Primary structure and characteristics of a lectin from skin mucus of the Japanese eel Anguilla japonica
    • S. Tasumi, T. Ohira, I. Kawazoe, H. Suetake, Y. Suzuki, and K. Aida Primary structure and characteristics of a lectin from skin mucus of the Japanese eel Anguilla japonica J. Biol. Chem. 277 2002 27305 27311
    • (2002) J. Biol. Chem. , vol.277 , pp. 27305-27311
    • Tasumi, S.1    Ohira, T.2    Kawazoe, I.3    Suetake, H.4    Suzuki, Y.5    Aida, K.6
  • 14
    • 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)
    • A.C. Mistry, S. Honda, and S. Hirose 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
  • 15
    • 0034670154 scopus 로고    scopus 로고
    • Cloning, mapping and genomic organization of a fish C-type lectin gene from homozygous clones of rainbow trout (Oncorhynchus mykiss)
    • H. Zhang, B. Robison, G.H. Thorgaard, and S.S. Ristow Cloning, mapping and genomic organization of a fish C-type lectin gene from homozygous clones of rainbow trout (Oncorhynchus mykiss) Biochim. Biophys. Acta 1494 2000 14 22
    • (2000) Biochim. Biophys. Acta , vol.1494 , pp. 14-22
    • Zhang, H.1    Robison, B.2    Thorgaard, G.H.3    Ristow, S.S.4
  • 16
    • 0033816605 scopus 로고    scopus 로고
    • The homologue of mannose-binding lectin in the carp family Cyprinidae is expressed at high level in spleen, and the deduced primary structure predicts affinity for galactose
    • L. Vitved, U. Holmskov, C. Koch, B. Teisner, S. Hansen, and K. Skjødt The homologue of mannose-binding lectin in the carp family Cyprinidae is expressed at high level in spleen, and the deduced primary structure predicts affinity for galactose Immunogenetics 51 2000 955 964
    • (2000) Immunogenetics , vol.51 , pp. 955-964
    • Vitved, L.1    Holmskov, U.2    Koch, C.3    Teisner, B.4    Hansen, S.5    Skjødt, K.6
  • 17
    • 0035315263 scopus 로고    scopus 로고
    • Molecular cloning of carp (Cyprinus carpio) C-type lectin and pentraxin by use of suppression subtractive hybridization
    • K. Fujiki, C.J. Bayne, D.H. Shin, M. Nakao, and T. Yano Molecular cloning of carp (Cyprinus carpio) C-type lectin and pentraxin by use of suppression subtractive hybridization Fish Shellfish Immunol. 11 2001 275 279
    • (2001) Fish Shellfish Immunol. , vol.11 , pp. 275-279
    • Fujiki, K.1    Bayne, C.J.2    Shin, D.H.3    Nakao, M.4    Yano, T.5
  • 18
    • 0035151325 scopus 로고    scopus 로고
    • Immune-relevant (including acute phase) genes identified in the livers of rainbow trout, Oncorhynchus mykiss, by means of suppression subtractive hybridization
    • C.J. Bayne, L. Gerwick, K. Fujiki, M. Nakao, and T. Yano Immune-relevant (including acute phase) genes identified in the livers of rainbow trout, Oncorhynchus mykiss, by means of suppression subtractive hybridization Dev. Comp. Immunol. 25 2001 205 217
    • (2001) Dev. Comp. Immunol. , vol.25 , pp. 205-217
    • Bayne, C.J.1    Gerwick, L.2    Fujiki, K.3    Nakao, M.4    Yano, T.5
  • 19
    • 24344447636 scopus 로고    scopus 로고
    • Three versions of the Fugu rubripes genome assembly are publicly available (http://fugu.hgmp.mrc.ac.uk ).
  • 20
    • 9444231673 scopus 로고    scopus 로고
    • C-type lectin-like domains in Fugu rubripes
    • A.N. Zelensky, and J.E. Gready C-type lectin-like domains in Fugu rubripes BMC Genomics 5 2004 51 (http://www.biomedcentral.com/1471-2164/5/51 )
    • (2004) BMC Genomics , vol.5 , pp. 51
    • Zelensky, A.N.1    Gready, J.E.2
  • 21
    • 84961040256 scopus 로고
    • Studies on fetuin, a glycoprotein of fetal serum: I. Isolation, chemical composition, and physicochemical properties
    • R.G. Spiro Studies on fetuin, a glycoprotein of fetal serum: I. Isolation, chemical composition, and physicochemical properties J. Biol. Chem. 235 1960 2860 2869
    • (1960) J. Biol. Chem. , vol.235 , pp. 2860-2869
    • Spiro, R.G.1
  • 22
    • 0016188434 scopus 로고
    • A simplified method for cyanogen bromide activation of agarose for affinity chromatography
    • S.C. March, I. Parikh, and P. Cuatrecasas A simplified method for cyanogen bromide activation of agarose for affinity chromatography Anal. Biochem. 60 1974 149 152
    • (1974) Anal. Biochem. , vol.60 , pp. 149-152
    • March, S.C.1    Parikh, I.2    Cuatrecasas, P.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature (London) 227 1970 680 685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0024249490 scopus 로고    scopus 로고
    • Comparative studies of the haemagglutination of adult and umbilical cord erythrocytes by animal lectins
    • K. Nitta, Y. Terasaki, H. Kawauchi, and G. Takayanagi Comparative studies of the haemagglutination of adult and umbilical cord erythrocytes by animal lectins Comp. Biochem. Physiol. 91B 1998 657 661
    • (1998) Comp. Biochem. Physiol. , vol.91 , pp. 657-661
    • Nitta, K.1    Terasaki, Y.2    Kawauchi, H.3    Takayanagi, G.4
  • 28
    • 0021678856 scopus 로고
    • A unique natural human IgG antibody with anti-alpha-galactosyl specificity
    • U. Galili, E.A. Rachmilewitz, A. Peleg, and I. Flechner A unique natural human IgG antibody with anti-alpha-galactosyl specificity J. Exp. Med. 160 1984 1519 1531
    • (1984) J. Exp. Med. , vol.160 , pp. 1519-1531
    • Galili, U.1    Rachmilewitz, E.A.2    Peleg, A.3    Flechner, I.4
  • 29
    • 0001044156 scopus 로고    scopus 로고
    • The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins
    • K.V. Ewart, Z. Li, D.S. Yang, G.L. Fletcher, and C.L. Hew 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
  • 30
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0017413222 scopus 로고
    • Five alpha-d-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds
    • L.A. Murphy, and I.J. Goldstein Five alpha-d-galactopyranosyl-binding isolectins from Bandeiraea simplicifolia seeds J. Biol. Chem. 252 1977 4739 4742
    • (1977) J. Biol. Chem. , vol.252 , pp. 4739-4742
    • Murphy, L.A.1    Goldstein, I.J.2
  • 33
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • P.Y. Chou, and G.D. Fasman Prediction of protein conformation Biochemistry 13 1974 222 245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 34
    • 0037424801 scopus 로고    scopus 로고
    • Cloning and characterization of the Atlantic salmon serum lectin, a long-form C-type lectin expressed in kidney
    • R.C. Richards, D.M. Hudson, P. Thibault, and K.V. Ewart 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
  • 36
    • 0036369409 scopus 로고    scopus 로고
    • Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-d-galactosamine-specific C-type lectin, CEL-I, from the holothuroidea, Cucumaria echinata
    • T. Hatakeyama, N. Matsuo, K. Shiba, S. Nishinohara, N. Yamasaki, H. Sugawara, and H. Aoyagi Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-d-galactosamine-specific C-type lectin, CEL-I, from the holothuroidea, Cucumaria echinata Biosci. Biotechnol. Biochem. 66 2002 157 163
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 157-163
    • Hatakeyama, T.1    Matsuo, N.2    Shiba, K.3    Nishinohara, S.4    Yamasaki, N.5    Sugawara, H.6    Aoyagi, H.7
  • 37
    • 0027177037 scopus 로고
    • Isolation and characterization of a cDNA encoding a Pleurodeles lectin
    • C. Tiffoche, A. Chesnel, P. Jego, and J.P. Le Pennec Isolation and characterization of a cDNA encoding a Pleurodeles lectin Eur. J. Biochem. 213 1993 901 907
    • (1993) Eur. J. Biochem. , vol.213 , pp. 901-907
    • Tiffoche, C.1    Chesnel, A.2    Jego, P.3    Le Pennec, J.P.4
  • 38
    • 0022844505 scopus 로고
    • Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein
    • K. Drickamer, M.S. Dordal, and L. Reynolds Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein J. Biol. Chem. 261 1986 6878 6887
    • (1986) J. Biol. Chem. , vol.261 , pp. 6878-6887
    • Drickamer, K.1    Dordal, M.S.2    Reynolds, L.3
  • 39
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • K. Drickamer Engineering galactose-binding activity into a C-type mannose-binding protein Nature (London) 360 1992 183 186
    • (1992) Nature (London) , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 40
    • 0034813966 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant nonglycosylated human serum transferrin containing a C-terminal hexahistidine tag
    • A.B. Mason, Q.Y. He, T.E. Adams, D.R. Gumerov, I.A. Kaltashov, V. Nguyen, and R.T. MacGillivray Expression, purification, and characterization of recombinant nonglycosylated human serum transferrin containing a C-terminal hexahistidine tag Protein Expr. Purif. 23 2001 142 150
    • (2001) Protein Expr. Purif. , vol.23 , pp. 142-150
    • Mason, A.B.1    He, Q.Y.2    Adams, T.E.3    Gumerov, D.R.4    Kaltashov, I.A.5    Nguyen, V.6    MacGillivray, R.T.7
  • 41
    • 0024443533 scopus 로고
    • Cystine-rich type II antifreeze protein precursor is initiated from the third AUG codon of its mRNA
    • P.H. Hayes, G.K. Scott, N.F. Ng, C.L. Hew, and P.L. Davies Cystine-rich type II antifreeze protein precursor is initiated from the third AUG codon of its mRNA J. Biol. Chem. 264 1989 18761 18767
    • (1989) J. Biol. Chem. , vol.264 , pp. 18761-18767
    • Hayes, P.H.1    Scott, G.K.2    Ng, N.F.3    Hew, C.L.4    Davies, P.L.5
  • 42
    • 0027507459 scopus 로고
    • Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca
    • Y. Usami, Y. Fujimura, M. Suzuki, Y. Ozeki, K. Nishio, H. Fukui, and K. Titani Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca Proc. Natl. Acad. Sci. U. S. A. 90 1993 928 932
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 928-932
    • Usami, Y.1    Fujimura, Y.2    Suzuki, M.3    Ozeki, Y.4    Nishio, K.5    Fukui, H.6    Titani, K.7
  • 43
    • 0024284252 scopus 로고
    • The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins
    • T.E. Petersen The amino-terminal domain of thrombomodulin and pancreatic stone protein are homologous with lectins FEBS Lett. 231 1988 51 53
    • (1988) FEBS Lett. , vol.231 , pp. 51-53
    • Petersen, T.E.1
  • 44
    • 0023159022 scopus 로고
    • Primary structure of tetranectin, a plasminogen kringle 4 binding plasma protein: Homology with asialoglycoprotein receptors and cartilage proteoglycan core protein
    • J. Fuhlendorff, I. Clemmensen, and S. Magnusson Primary structure of tetranectin, a plasminogen kringle 4 binding plasma protein: homology with asialoglycoprotein receptors and cartilage proteoglycan core protein Biochemistry 26 1987 6757 6764
    • (1987) Biochemistry , vol.26 , pp. 6757-6764
    • Fuhlendorff, J.1    Clemmensen, I.2    Magnusson, S.3
  • 45
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • W.I. Weis, K. Drickamer, and W.A. Hendrickson Structure of a C-type mannose-binding protein complexed with an oligosaccharide Nature (London) 360 1992 127 134
    • (1992) Nature (London) , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 46
    • 0021690855 scopus 로고
    • Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal signal sequence
    • E.C. Holland, J.O. Leung, and K. Drickamer Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal signal sequence Proc. Natl. Acad. Sci. U. S. A. 81 1984 7338 7342
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 7338-7342
    • Holland, E.C.1    Leung, J.O.2    Drickamer, K.3
  • 47
    • 0025967119 scopus 로고
    • Structure of the gene for a carbohydrate-binding receptor unique to rat Kupffer cells
    • G.W. Hoyle, and R.L. Hill Structure of the gene for a carbohydrate-binding receptor unique to rat Kupffer cells J. Biol. Chem. 266 1991 1850 1857
    • (1991) J. Biol. Chem. , vol.266 , pp. 1850-1857
    • Hoyle, G.W.1    Hill, R.L.2
  • 48
    • 0025740531 scopus 로고
    • A novel functional cell surface dimer (Kp43) expressed by natural killer cells and gamma/delta TCR+T lymphocytes: II. Modulation of natural killer cytotoxicity by anti-Kp43 monoclonal antibody
    • J. Aramburu, M.A. Balboa, M. Izquierdo, and M. Lopez-Botet A novel functional cell surface dimer (Kp43) expressed by natural killer cells and gamma/delta TCR+T lymphocytes: II. Modulation of natural killer cytotoxicity by anti-Kp43 monoclonal antibody J. Immunol. 147 1991 714 721
    • (1991) J. Immunol. , vol.147 , pp. 714-721
    • Aramburu, J.1    Balboa, M.A.2    Izquierdo, M.3    Lopez-Botet, M.4
  • 49
    • 0025754310 scopus 로고
    • DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells
    • J.P. Houchins, T. Yabe, C. McSherry, and F.H. Bach DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells J. Exp. Med. 173 1991 1017 1020
    • (1991) J. Exp. Med. , vol.173 , pp. 1017-1020
    • Houchins, J.P.1    Yabe, T.2    McSherry, C.3    Bach, F.H.4
  • 50
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.