메뉴 건너뛰기




Volumn 9, Issue 2, 1997, Pages 203-210

Characterization of human lactoferrin produced in the baculovirus expression system

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; LEPIDOPTERA; MYTHIMNA UNIPUNCTA; SPODOPTERA FRUGIPERDA; UNIDENTIFIED BACULOVIRUS;

EID: 0031104985     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0687     Document Type: Article
Times cited : (46)

References (44)
  • 1
    • 0001213833 scopus 로고
    • Préparation et propriétés de la lactosidérophiline (lactotransferrine) du lait de Femme
    • Montreuil J., Tonnelat J., Mullet S. Préparation et propriétés de la lactosidérophiline (lactotransferrine) du lait de Femme. Biochim. Biophys. Acta. 45:1960;413-421.
    • (1960) Biochim. Biophys. Acta , vol.45 , pp. 413-421
    • Montreuil, J.1    Tonnelat, J.2    Mullet, S.3
  • 2
    • 0009665799 scopus 로고
    • An iron-binding protein common to many external secretions
    • Masson P. L., Heremans J. F., Dive C. An iron-binding protein common to many external secretions. Clin. Chim. Acta. 14:1966;735-739.
    • (1966) Clin. Chim. Acta , vol.14 , pp. 735-739
    • Masson, P.L.1    Heremans, J.F.2    Dive, C.3
  • 3
    • 0014574791 scopus 로고
    • Lactoferrin, an iron binding protein in neutrophilic leukocytes
    • Masson P. L., Heremans J. F., Schonne E. Lactoferrin, an iron binding protein in neutrophilic leukocytes. J. Exp. Med. 130:1969;643-657.
    • (1969) J. Exp. Med. , vol.130 , pp. 643-657
    • Masson, P.L.1    Heremans, J.F.2    Schonne, E.3
  • 7
    • 0025367328 scopus 로고
    • Nucleotide sequence of human lactoferrin cDNA
    • Powell M. J., Ogden J. E. Nucleotide sequence of human lactoferrin cDNA. Nucleic Acids Res. 18:1990;4013.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4013
    • Powell, M.J.1    Ogden, J.E.2
  • 8
    • 0028813886 scopus 로고
    • Structure of human diferric lactoferrin refined at 2.2 resolution
    • Haridas M., Anderson B. F., Baker E. N. Structure of human diferric lactoferrin refined at 2.2 resolution. Acta Crystallogr. 51:1995;629-646.
    • (1995) Acta Crystallogr. , vol.51 , pp. 629-646
    • Haridas, M.1    Anderson, B.F.2    Baker, E.N.3
  • 10
    • 0343469199 scopus 로고    scopus 로고
    • Transferrin superfamily. An outstanding model for studying biochemical evolution
    • Amsterdam: Elsevier
    • Montreuil J., Spik G., Mazurier J. Transferrin superfamily. An outstanding model for studying biochemical evolution. Glycoproteins. 1997;Elsevier, Amsterdam.
    • (1997) Glycoproteins
    • Montreuil, J.1    Spik, G.2    Mazurier, J.3
  • 11
    • 0018179083 scopus 로고
    • Bacteriostasis of a milk-sensitive strain ofEscherichia coli
    • Spik G., Chéron A., Montreuil J., Dolby J. Bacteriostasis of a milk-sensitive strain ofEscherichia coli. Immunology. 35:1978;663-671.
    • (1978) Immunology , vol.35 , pp. 663-671
    • Spik, G.1    Chéron, A.2    Montreuil, J.3    Dolby, J.4
  • 12
    • 0018132103 scopus 로고
    • Identification of lactoferrin as the granulocyte-derived inhibitor of colony stimulating activity (CSA)-production
    • Broxmeyer H. E., Smithyman A., Eger R. R., Meyers P. A., de Sousa M. Identification of lactoferrin as the granulocyte-derived inhibitor of colony stimulating activity (CSA)-production. J. Exp. Med. 148:1978;1052-1067.
    • (1978) J. Exp. Med. , vol.148 , pp. 1052-1067
    • Broxmeyer, H.E.1    Smithyman, A.2    Eger, R.R.3    Meyers, P.A.4    De Sousa, M.5
  • 13
    • 0024468617 scopus 로고
    • Lactoferrin decreases monocyte-induced fibroblast production of myeloid colony-stimulating activity by suppressing monocyte release of interleukin-1
    • Zucali J. R., Broxmeyer H. E., Levy D., Morse C. Lactoferrin decreases monocyte-induced fibroblast production of myeloid colony-stimulating activity by suppressing monocyte release of interleukin-1. Blood. 74:1989;1531-1536.
    • (1989) Blood , vol.74 , pp. 1531-1536
    • Zucali, J.R.1    Broxmeyer, H.E.2    Levy, D.3    Morse, C.4
  • 14
    • 0019467167 scopus 로고
    • Lactoferrin-mediated modulation of mononuclear cell activities
    • Duncan R. H., McArthur W. P. Lactoferrin-mediated modulation of mononuclear cell activities. Cell Immunol. 63:1981;308-320.
    • (1981) Cell Immunol. , vol.63 , pp. 308-320
    • Duncan, R.H.1    McArthur, W.P.2
  • 15
    • 0021059044 scopus 로고
    • Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium
    • Hashizume S., Kuroda K., Murakami H. Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium. Biochim. Biophys. Acta. 763:1983;377-382.
    • (1983) Biochim. Biophys. Acta , vol.763 , pp. 377-382
    • Hashizume, S.1    Kuroda, K.2    Murakami, H.3
  • 16
    • 0024586305 scopus 로고
    • Expression of human lactotransferrin receptors in phytohemagglutinin-stimulated human peripheral blood lymphocytes. Isolation of the receptors by anti-ligand affinity chromatography
    • Mazurier J., Legrand D., Hu W. L., Montreuil J., Spik G. Expression of human lactotransferrin receptors in phytohemagglutinin-stimulated human peripheral blood lymphocytes. Isolation of the receptors by anti-ligand affinity chromatography. Eur. J. Biochem. 179:1989;481-487.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 481-487
    • Mazurier, J.1    Legrand, D.2    Hu, W.L.3    Montreuil, J.4    Spik, G.5
  • 18
    • 0029145713 scopus 로고
    • Human lactoferrin induces phenotypic and functional changes in murine splenic B cells
    • Zimecki M., Mazurier J., Spik G., Kapp J. A. Human lactoferrin induces phenotypic and functional changes in murine splenic B cells. Immunology. 86:1995;122-127.
    • (1995) Immunology , vol.86 , pp. 122-127
    • Zimecki, M.1    Mazurier, J.2    Spik, G.3    Kapp, J.A.4
  • 20
    • 0018633103 scopus 로고
    • Iron-binding proteins and influx of iron across the duodenal brush border. Evidence for specific lactotransferrin receptors in the human intestine
    • Cox T. M., Mazurier J., Spik G., Montreuil J., Peters T. J. Iron-binding proteins and influx of iron across the duodenal brush border. Evidence for specific lactotransferrin receptors in the human intestine. Biochim. Biophys. Acta. 588:1979;120-128.
    • (1979) Biochim. Biophys. Acta , vol.588 , pp. 120-128
    • Cox, T.M.1    Mazurier, J.2    Spik, G.3    Montreuil, J.4    Peters, T.J.5
  • 21
    • 0029002524 scopus 로고
    • Effect of intracellular iron depletion by picolinic acid on expression of the lactoferrin receptor in the human colon carcinoma cell subclone HT29-18-C-1
    • Mikogami T., Marianne T., Spik G. Effect of intracellular iron depletion by picolinic acid on expression of the lactoferrin receptor in the human colon carcinoma cell subclone HT29-18-C-1. Biochem. J. 308:1995;391-397.
    • (1995) Biochem. J. , vol.308 , pp. 391-397
    • Mikogami, T.1    Marianne, T.2    Spik, G.3
  • 22
    • 0027749110 scopus 로고
    • Endocytosis and degradation of bovine apo- And holo-lactoferrin by isolated rat hepatocytes are mediated by calcium-dependent recycling binding sites
    • McAbee D. D., Nowatzke W., Oehler C., Sitaram M., Sbaschnig E., Opferman J. T., Carr J., Esbensen K. Endocytosis and degradation of bovine apo- and holo-lactoferrin by isolated rat hepatocytes are mediated by calcium-dependent recycling binding sites. Biochemistry. 32:1993;13749-13760.
    • (1993) Biochemistry , vol.32 , pp. 13749-13760
    • McAbee, D.D.1    Nowatzke, W.2    Oehler, C.3    Sitaram, M.4    Sbaschnig, E.5    Opferman, J.T.6    Carr, J.7    Esbensen, K.8
  • 23
    • 0027787983 scopus 로고
    • Removal of 14 N-terminal amino acids of lactoferrin enhances its affinity for parenchymal liver cells and potentiates the inhibition of β-very low density lipoprotein binding
    • Ziere G. J., Kruiit J. K., Bijsterbosch M. K., van Berkel T. J. C. Removal of 14 N-terminal amino acids of lactoferrin enhances its affinity for parenchymal liver cells and potentiates the inhibition of β-very low density lipoprotein binding. J. Biol. Chem. 268:1993;27069-27075.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27069-27075
    • Ziere, G.J.1    Kruiit, J.K.2    Bijsterbosch, M.K.3    Van Berkel, T.J.C.4
  • 24
    • 0027075914 scopus 로고
    • Characterization of lactotransferrin receptor in epithelial cell lines from non-malignant human breast, benign mastopathies and breast carcinomas
    • Rochard E., Legrand D., Lecocq M., Hamelin R., Crépin M., Montreuil J., Spik G. Characterization of lactotransferrin receptor in epithelial cell lines from non-malignant human breast, benign mastopathies and breast carcinomas. Anticancer Res. 12:1992;2047-2052.
    • (1992) Anticancer Res. , vol.12 , pp. 2047-2052
    • Rochard, E.1    Legrand, D.2    Lecocq, M.3    Hamelin, R.4    Crépin, M.5    Montreuil, J.6    Spik, G.7
  • 25
    • 0026803187 scopus 로고
    • Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain-I of human lactotransferrin
    • Legrand D., Mazurier J., Elass A., Rochard E., Vergoten G., Maes P., Montreuil J., Spik G. Molecular interactions between human lactotransferrin and the phytohemagglutinin-activated human lymphocyte lactotransferrin receptor lie in two loop-containing regions of the N-terminal domain-I of human lactotransferrin. Biochemistry. 31:1992;9243-9251.
    • (1992) Biochemistry , vol.31 , pp. 9243-9251
    • Legrand, D.1    Mazurier, J.2    Elass, A.3    Rochard, E.4    Vergoten, G.5    Maes, P.6    Montreuil, J.7    Spik, G.8
  • 26
    • 0029043238 scopus 로고
    • Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells
    • Legrand D., Salmon V., Coddeville B., Benaïssa M., Plancke Y., Spik G. Structural determination of two N-linked glycans isolated from recombinant human lactoferrin expressed in BHK cells. FEBS Lett. 365:1995;57-60.
    • (1995) FEBS Lett. , vol.365 , pp. 57-60
    • Legrand, D.1    Salmon, V.2    Coddeville, B.3    Benaïssa, M.4    Plancke, Y.5    Spik, G.6
  • 27
    • 0029620277 scopus 로고
    • Lactoferrin-lipopolysaccharide interaction: Involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding toEscherichia coli
    • Elass-Rochard E., Roseanu A., Legrand D., Trif M., Salmon V., Motas C., Montreuil J., Spik G. Lactoferrin-lipopolysaccharide interaction: Involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding toEscherichia coli. Biochem. J. 312:1995;839-845.
    • (1995) Biochem. J. , vol.312 , pp. 839-845
    • Elass-Rochard, E.1    Roseanu, A.2    Legrand, D.3    Trif, M.4    Salmon, V.5    Motas, C.6    Montreuil, J.7    Spik, G.8
  • 28
    • 0023881356 scopus 로고
    • Trends in the development of baculovirus expression vectors
    • Luckow V. A., Summers M. D. Trends in the development of baculovirus expression vectors. Biotechnology. 6:1988;47-55.
    • (1988) Biotechnology , vol.6 , pp. 47-55
    • Luckow, V.A.1    Summers, M.D.2
  • 29
    • 0025726727 scopus 로고
    • Expression of biologically active human antithrombin III by recombinant baculovirus inSpodoptera frugiperda
    • Gillepsie L. S., Hilesland K. K., Kanuer D. J. Expression of biologically active human antithrombin III by recombinant baculovirus inSpodoptera frugiperda. J. Biol. Chem. 266:1991;3995-4001.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3995-4001
    • Gillepsie, L.S.1    Hilesland, K.K.2    Kanuer, D.J.3
  • 30
    • 14744303350 scopus 로고
    • Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion
    • Davis T. R., Trotter K. M., Grandos R. R., Wood H. A. Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion. Biotechnology. 10:1992;1148-1150.
    • (1992) Biotechnology , vol.10 , pp. 1148-1150
    • Davis, T.R.1    Trotter, K.M.2    Grandos, R.R.3    Wood, H.A.4
  • 32
    • 0028025037 scopus 로고
    • Apical to basolateral transcytosis of human lactoferrin in human differentiated colon carcinoma cell clone HT-29cl 19A
    • Mikogami T., Heyman M., Spik G., Desjeux J. F. Apical to basolateral transcytosis of human lactoferrin in human differentiated colon carcinoma cell clone HT-29cl 19A. J. Am. Physiol. 267:1994;G308-G315.
    • (1994) J. Am. Physiol. , vol.267
    • Mikogami, T.1    Heyman, M.2    Spik, G.3    Desjeux, J.F.4
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T-4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T-4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0019153180 scopus 로고
    • Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin
    • Mazurier J., Spik G. Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin. Biochim. Biophys. Acta. 629:1980;399-408.
    • (1980) Biochim. Biophys. Acta , vol.629 , pp. 399-408
    • Mazurier, J.1    Spik, G.2
  • 35
    • 0015494930 scopus 로고
    • Analysis of monosaccharides by gas-liquid chromatography of theO
    • Zanetta J. P., Breckenridge W. C., Vincendon G. Analysis of monosaccharides by gas-liquid chromatography of theO. J. Chromatogr. 69:1972;291-304.
    • (1972) J. Chromatogr. , vol.69 , pp. 291-304
    • Zanetta, J.P.1    Breckenridge, W.C.2    Vincendon, G.3
  • 36
    • 0016758296 scopus 로고
    • Characterization by gas liquid chromatography, mass spectrometry of per-trimethylsilyl glycosides obtained in the methanolysis of glycoproteins and glycolipids
    • Kamerling J. P., Gerwig G. J., Vliegenthart J. F. G., Clamp J. R. Characterization by gas liquid chromatography, mass spectrometry of per-trimethylsilyl glycosides obtained in the methanolysis of glycoproteins and glycolipids. Biochem. J. 151:1975;491-495.
    • (1975) Biochem. J. , vol.151 , pp. 491-495
    • Kamerling, J.P.1    Gerwig, G.J.2    Vliegenthart, J.F.G.3    Clamp, J.R.4
  • 38
    • 0025783212 scopus 로고
    • Expression of cloned human lactoferrin in baby-hamster kidney cells
    • Stowell K. M., Rado T. A., Funk W. D., Tweedie J. W. Expression of cloned human lactoferrin in baby-hamster kidney cells. Biochem. J. 276:1991;349-355.
    • (1991) Biochem. J. , vol.276 , pp. 349-355
    • Stowell, K.M.1    Rado, T.A.2    Funk, W.D.3    Tweedie, J.W.4
  • 39
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard G. The attractions of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 51:1949;660-672.
    • (1949) Ann. N.Y. Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 40
    • 14744300639 scopus 로고
    • Production of biologically active recombinant human lactoferrin inAspergillus oryzae
    • Ward P. P., Lo J. Y., Duke M., May G. S., Headon D. R., Conneely O. M. Production of biologically active recombinant human lactoferrin inAspergillus oryzae. Biotechnology. 10:1992;784-789.
    • (1992) Biotechnology , vol.10 , pp. 784-789
    • Ward, P.P.1    Lo, J.Y.2    Duke, M.3    May, G.S.4    Headon, D.R.5    Conneely, O.M.6
  • 41
    • 0026448560 scopus 로고
    • An inducible expression system for the production of human lactoferrin inAspergillus nidulans
    • Ward P. P., May G. S., Headon D. R., Conneely O. M. An inducible expression system for the production of human lactoferrin inAspergillus nidulans. Gene. 122:1992;219-223.
    • (1992) Gene , vol.122 , pp. 219-223
    • Ward, P.P.1    May, G.S.2    Headon, D.R.3    Conneely, O.M.4
  • 42
    • 0000452573 scopus 로고
    • Expression and characterization of human lactoferrin in yeastSaccharomyces cerevisiae
    • Liang Q. W., Richardson T. Expression and characterization of human lactoferrin in yeastSaccharomyces cerevisiae. J. Agric. Food Chem. 41:1993;1800-1807.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1800-1807
    • Liang, Q.W.1    Richardson, T.2
  • 43
    • 0023050642 scopus 로고
    • The purification of eucaryotic polypeptides synthesized inEscherichia coli
    • Marston F. A. O. The purification of eucaryotic polypeptides synthesized inEscherichia coli. Biochem. J. 240:1986;1-12.
    • (1986) Biochem. J. , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 44
    • 0025139279 scopus 로고
    • Isolation and partial characterization of a lactotransferrin receptor from mouse intestinal brush border
    • Hu W. L., Mazurier J., Montreuil J., Spik G. Isolation and partial characterization of a lactotransferrin receptor from mouse intestinal brush border. Biochemistry. 29:1990;535-541.
    • (1990) Biochemistry , vol.29 , pp. 535-541
    • Hu, W.L.1    Mazurier, J.2    Montreuil, J.3    Spik, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.