메뉴 건너뛰기




Volumn 204, Issue 1-2, 1997, Pages 171-176

Expression and characterization of recombinant murine lactoferrin

Author keywords

Aspergillus; Iron binding

Indexed keywords

IRON; LACTOFERRIN; RECOMBINANT PROTEIN;

EID: 0031578704     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00539-8     Document Type: Article
Times cited : (22)

References (56)
  • 1
    • 0018850440 scopus 로고
    • Iron transport and storage proteins
    • Aisen P., Listowsky I. Iron transport and storage proteins. Annu. Rev. Biochem. 49:1980;357-393.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 357-393
    • Aisen, P.1    Listowsky, I.2
  • 2
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8Å resolution
    • Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N. Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8Å resolution. J. Mol. Biol. 209:1989;711-734.
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 3
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • Arnold R.R., Cole M.F., McGhee J.R. A bactericidal effect for human lactoferrin. Science. 197:1977;263-265.
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 7
    • 0015497562 scopus 로고
    • Iron-binding proteins in milk and resistance to Escherichia coli infections in infants
    • Bullen J.J., Rogers H.J., Leigh L. Iron-binding proteins in milk and resistance to Escherichia coli infections in infants. Br. Med. J. 1:1971;69-75.
    • (1971) Br. Med. J. , vol.1 , pp. 69-75
    • Bullen, J.J.1    Rogers, H.J.2    Leigh, L.3
  • 8
    • 0141743120 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. 558:1979;129-141.
    • (1979) Biochim. Biophys. Acta , vol.558 , pp. 129-141
    • Cox, T.M.1    Mazurier, J.2    Spik, G.3    Montreuil, J.4    Peters, T.J.5
  • 9
    • 0026716209 scopus 로고
    • Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin
    • Crouch S.P.M., Slater K.J., Fletcher J. Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin. Blood. 80:1992;235-240.
    • (1992) Blood , vol.80 , pp. 235-240
    • Crouch, S.P.M.1    Slater, K.J.2    Fletcher, J.3
  • 10
    • 0024803796 scopus 로고
    • Fe-saturation and proteolysis of human lactoferrin: Effect on brush-border receptor-mediated uptake of Fe and Mn
    • Davidson L.A., Lonnerdal B. Fe-saturation and proteolysis of human lactoferrin: effect on brush-border receptor-mediated uptake of Fe and Mn. Am. J. Physiol. 257:1989;G930-G934.
    • (1989) Am. J. Physiol. , vol.257
    • Davidson, L.A.1    Lonnerdal, B.2
  • 11
    • 0024269170 scopus 로고
    • An efficient cell-free translation system from Aspergillus nidulans and in vitro translocation of prepro-a mating factor across Aspergillus microsomes
    • Devchand M., Gwynne D.I., Buxton F., Davies R. An efficient cell-free translation system from Aspergillus nidulans and in vitro translocation of prepro-a mating factor across Aspergillus microsomes. Curr. Genet. 14:1989;561-566.
    • (1989) Curr. Genet. , vol.14 , pp. 561-566
    • Devchand, M.1    Gwynne, D.I.2    Buxton, F.3    Davies, R.4
  • 12
    • 0026095436 scopus 로고
    • Killing of gram-negative bacteria by lactoferrin and lysozyme
    • Ellison R.T., Giehl T.J. Killing of gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest. 88:1991;1080-1091.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1080-1091
    • Ellison, R.T.1    Giehl, T.J.2
  • 14
    • 0001395327 scopus 로고
    • The isolation of a red protein from milk
    • Groves M.L. The isolation of a red protein from milk. J. Am. Chem. Soc. 82:1960;3345-3350.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3345-3350
    • Groves, M.L.1
  • 15
    • 0025833024 scopus 로고
    • Influence of T-lymphocytes and lactoferrin on the survival promoting effects of IL-1 and IL-6 on human bone marrow granulocyte-macrophage and erythroid progenitor cells
    • Hangoc G., Falkenburg J.H.F., Broxmeyer H.E. Influence of T-lymphocytes and lactoferrin on the survival promoting effects of IL-1 and IL-6 on human bone marrow granulocyte-macrophage and erythroid progenitor cells. Exp. Hematol. 19:1991;697-703.
    • (1991) Exp. Hematol. , vol.19 , pp. 697-703
    • Hangoc, G.1    Falkenburg, J.H.F.2    Broxmeyer, H.E.3
  • 16
    • 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 M. Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium. Biochem. Biophys. Res. Commun. 763:1983;377-382.
    • (1983) Biochem. Biophys. Res. Commun. , vol.763 , pp. 377-382
    • Hashizume, S.1    Kuroda, K.2    Murakami, M.3
  • 17
    • 0023079986 scopus 로고
    • Cell culture assay of biological activity of lactoferrin and transferrin
    • Hashizume S., Kuroda K., Murakami H. Cell culture assay of biological activity of lactoferrin and transferrin. Meth. Enzymol. 147:1987;302-314.
    • (1987) Meth. Enzymol. , vol.147 , pp. 302-314
    • Hashizume, S.1    Kuroda, K.2    Murakami, H.3
  • 18
    • 0028910517 scopus 로고
    • Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA
    • He J., Furmanski P. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature. 373:1995;721-724.
    • (1995) Nature , vol.373 , pp. 721-724
    • He, J.1    Furmanski, P.2
  • 19
    • 0025957064 scopus 로고
    • Lysozyme, lactoferrin and secretory immunoglobin A content in breast milk: Influence of duration of lactation, nutrition status, prolactin status, and parity of mother
    • Hennart P.F., Brasseur D.J., Delogne-Desnoeck J.B., Dramaix M.M., Robyn C.E. Lysozyme, lactoferrin and secretory immunoglobin A content in breast milk: influence of duration of lactation, nutrition status, prolactin status, and parity of mother. Am. J. Clin. Nutr. 53:1991;32-39.
    • (1991) Am. J. Clin. Nutr. , vol.53 , pp. 32-39
    • Hennart, P.F.1    Brasseur, D.J.2    Delogne-Desnoeck, J.B.3    Dramaix, M.M.4    Robyn, C.E.5
  • 20
    • 0024286454 scopus 로고
    • Lactotransferrin receptor of mouse small-intestinal brush border: Binding characteristics of membrane-bound and Triton X-100-solubilized forms
    • Hu W.-L., Mazurier J., Sawatzki G., Montreuil J., Spik G. Lactotransferrin receptor of mouse small-intestinal brush border: binding characteristics of membrane-bound and Triton X-100-solubilized forms. Biochem. J. 249:1988;435-441.
    • (1988) Biochem. J. , vol.249 , pp. 435-441
    • Hu, W.-L.1    Mazurier, J.2    Sawatzki, G.3    Montreuil, J.4    Spik, G.5
  • 21
    • 0025139279 scopus 로고
    • Isolation and partial characterization of a lactotransferrin receptor from mouse intestinal brush border
    • Hu W.-L., Mazurier 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    Spik, G.3
  • 22
    • 0027378892 scopus 로고
    • Binding of lactoferrin and transferrin to the human promonocytic cell line
    • Ismail M., Brock J.H. Binding of lactoferrin and transferrin to the human promonocytic cell line. J. Biol. Chem. 268:1993;21618-21625.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21618-21625
    • Ismail, M.1    Brock, J.H.2
  • 23
    • 0027467647 scopus 로고
    • Lactoferrin, lactoferrin receptors and iron metabolism
    • Iyer S., Lonnerdal B. Lactoferrin, lactoferrin receptors and iron metabolism. Eur. J. Clin. Nutr. 47:1993;232-241.
    • (1993) Eur. J. Clin. Nutr. , vol.47 , pp. 232-241
    • Iyer, S.1    Lonnerdal, B.2
  • 24
    • 0020092046 scopus 로고
    • The complete nucleotide sequence of the chick ovotransferrin mRNA
    • Jeltsch J.-M., Chambon P. The complete nucleotide sequence of the chick ovotransferrin mRNA. Eur. J. Biochem. 122:1982;291-295.
    • (1982) Eur. J. Biochem. , vol.122 , pp. 291-295
    • Jeltsch, J.-M.1    Chambon, P.2
  • 25
    • 0026331372 scopus 로고
    • Isolation and function of a receptor for human lactoferrin in human fetal intestinal brush-border membrane
    • Kawakami H., Lonnedal B. Isolation and function of a receptor for human lactoferrin in human fetal intestinal brush-border membrane. Am. J. Physiol. 261:1991;G841-G846.
    • (1991) Am. J. Physiol. , vol.261
    • Kawakami, H.1    Lonnedal, B.2
  • 26
    • 0029130333 scopus 로고
    • Lactoferrin molecular structure and biological function
    • Lonnerdal B., Iyer S. Lactoferrin molecular structure and biological function. Annu. Rev. Nutr. 15:1995;93-110.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 93-110
    • Lonnerdal, B.1    Iyer, S.2
  • 28
    • 0027515007 scopus 로고
    • Lactoferrin regulates the release of tumour necrosis factor alpha and interleukin 6 in vivo
    • Machnicki M., Zimecki M., Zagulski T. Lactoferrin regulates the release of tumour necrosis factor alpha and interleukin 6 in vivo. Int. J. Exp. Path. 74:1993;433-439.
    • (1993) Int. J. Exp. Path. , vol.74 , pp. 433-439
    • MacHnicki, M.1    Zimecki, M.2    Zagulski, T.3
  • 29
    • 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
  • 30
    • 0013968292 scopus 로고
    • Immunohistochemical localization and bacteriostatic properties of an iron binding protein from bronchial mucus
    • Masson P.L., Heremans J.F., Priguot J.J., Wauters G. Immunohistochemical localization and bacteriostatic properties of an iron binding protein from bronchial mucus. Thorax. 21:1966;538-544.
    • (1966) Thorax , vol.21 , pp. 538-544
    • Masson, P.L.1    Heremans, J.F.2    Priguot, J.J.3    Wauters, G.4
  • 31
    • 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;643-658.
    • (1969) J. Exp. Med. , vol.130 , pp. 643-658
    • Masson, P.L.1    Heremans, J.F.2    Schonne, E.3
  • 32
    • 0014404173 scopus 로고
    • Metal-combining properties of human lactoferrin (Red Milk Protein). 1. The involvement of bicarbonate in the reaction
    • Masson P.L., Heremans J.F. Metal-combining properties of human lactoferrin (Red Milk Protein). 1. The involvement of bicarbonate in the reaction. Eur. J. Biochem. 6:1968;579-584.
    • (1968) Eur. J. Biochem. , vol.6 , pp. 579-584
    • Masson, P.L.1    Heremans, J.F.2
  • 34
    • 0024586305 scopus 로고
    • Expression of human lactotransferrin receptors in phytohemagglutinin stimulated human peripheral blood lymphocytes: Isolation of the receptors by antiligand-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 antiligand-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
  • 36
    • 0021975789 scopus 로고
    • The biological role of lactoferrin
    • Nemet K., Simonovits I. The biological role of lactoferrin. Haematologia. 18:1985;3-12.
    • (1985) Haematologia , vol.18 , pp. 3-12
    • Nemet, K.1    Simonovits, I.2
  • 37
    • 0023228506 scopus 로고
    • Human lactoferrin stimulates thymidine incorporation into DNA of rat crypt cells
    • Nichols B.L., McKee K., Henry J.F., Putman M. Human lactoferrin stimulates thymidine incorporation into DNA of rat crypt cells. Pediatr. Res. 21:1987;563-567.
    • (1987) Pediatr. Res. , vol.21 , pp. 563-567
    • Nichols, B.L.1    McKee, K.2    Henry, J.F.3    Putman, M.4
  • 38
    • 0025357468 scopus 로고
    • Iron is not required in the lactoferrin stimulation of thymidine incorporation into the DNA of rat crypt enterocytes
    • Nichols B.L., McKee K.S., Huebers H.A. Iron is not required in the lactoferrin stimulation of thymidine incorporation into the DNA of rat crypt enterocytes. Pediatr. Res. 27:1990;525-528.
    • (1990) Pediatr. Res. , vol.27 , pp. 525-528
    • Nichols, B.L.1    McKee, K.S.2    Huebers, H.A.3
  • 39
    • 0014428034 scopus 로고
    • Inhibition of bacteria by lactoferrin and other iron-chelating agents
    • Oram J.D., Reiter B. Inhibition of bacteria by lactoferrin and other iron-chelating agents. Biochim. Biophys. Acta. 170:1968;351-365.
    • (1968) Biochim. Biophys. Acta , vol.170 , pp. 351-365
    • Oram, J.D.1    Reiter, B.2
  • 40
    • 0029012726 scopus 로고
    • Lactoferrin down-modulates the activity of the granulocyte macrophage colony-stimulating factor promoter in interleukin-1 beta-stimulated cells
    • Penco S., Pastorino S., Bianchi S.G., Garre C. Lactoferrin down-modulates the activity of the granulocyte macrophage colony-stimulating factor promoter in interleukin-1 beta-stimulated cells. J. Biol. Chem. 270:1995;12263-12268.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12263-12268
    • Penco, S.1    Pastorino, S.2    Bianchi, S.G.3    Garre, C.4
  • 41
    • 0023664683 scopus 로고
    • Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions
    • Pentecost B.T., Teng C.T. Lactotransferrin is the major estrogen inducible protein of mouse uterine secretions. J. Biol. Chem. 262:1987;10134-10139.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10134-10139
    • Pentecost, B.T.1    Teng, C.T.2
  • 42
  • 43
    • 0024473916 scopus 로고
    • Lactoferrin stimulates colony stimulating factor production in vitro and in vivo
    • Sawatzki G., Rich C. Lactoferrin stimulates colony stimulating factor production in vitro and in vivo. Blood Cells. 15:1989;371-375.
    • (1989) Blood Cells , vol.15 , pp. 371-375
    • Sawatzki, G.1    Rich, C.2
  • 44
    • 0024119835 scopus 로고
    • Comparative study of the primary structures of sero-, lacto- And ovatransferrin glycans from different species
    • Spik G., Coddenville B., Montreuil J. Comparative study of the primary structures of sero-, lacto- and ovatransferrin glycans from different species. Biochemistry. 70:1988;1459-1469.
    • (1988) Biochemistry , vol.70 , pp. 1459-1469
    • Spik, G.1    Coddenville, B.2    Montreuil, J.3
  • 45
    • 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
  • 46
    • 0029026622 scopus 로고
    • A system for production of commercial quantities of human lactoferrin; A broad spectrum natural antibiotic
    • Ward P.P., Piddington C.S., Cunningham G.A., Zhou X., Wyatt R.D., Conneely O.M. A system for production of commercial quantities of human lactoferrin; a broad spectrum natural antibiotic. Biotechnology. 13:1995;498-503.
    • (1995) Biotechnology , vol.13 , pp. 498-503
    • Ward, P.P.1    Piddington, C.S.2    Cunningham, G.A.3    Zhou, X.4    Wyatt, R.D.5    Conneely, O.M.6
  • 47
    • 17544364169 scopus 로고    scopus 로고
    • Cooperative interactions between the amino- And carboxyl-terminal lobes contribute to the unique iron-binding stability of lactoferrin
    • Ward P.P., Zhou X., Conneely O.M. Cooperative interactions between the amino- and carboxyl-terminal lobes contribute to the unique iron-binding stability of lactoferrin. J. Biol. Chem. 271:1996;12790-12794.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12790-12794
    • Ward, P.P.1    Zhou, X.2    Conneely, O.M.3
  • 48
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg E.D. Iron and infection. Microbiol. Rev. 42:1978;45-66.
    • (1978) Microbiol. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 49
    • 0018775954 scopus 로고
    • Secretory responses of human neutrophils: Exocytosis of specific (secondary) granules by human neutrophils during adherence in vitro and during exudation in vivo
    • Wright D.G., Gallin J.I. Secretory responses of human neutrophils: exocytosis of specific (secondary) granules by human neutrophils during adherence in vitro and during exudation in vivo. J. Immunol. 123:1979;285-294.
    • (1979) J. Immunol. , vol.123 , pp. 285-294
    • Wright, D.G.1    Gallin, J.I.2
  • 50
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi K., Tomita M., Giehl T.J., Ellison R.T. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:1993;719-728.
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison, R.T.4
  • 52
    • 0027360302 scopus 로고
    • The developmental profile of lactoferrin
    • Yu L.-C., Chen Y.-H. The developmental profile of lactoferrin. Biochem. J. 296:1993;107-111.
    • (1993) Biochem. J. , vol.296 , pp. 107-111
    • Yu, L.-C.1    Chen, Y.-H.2
  • 53
    • 0024842051 scopus 로고
    • Lactoferrin can protect mice against a lethal dose of Escherichia coli in experimental infection in vivo
    • Zagulski T., Lipinski P., Zagulska A., Broniek S., Jarzabek Z. Lactoferrin can protect mice against a lethal dose of Escherichia coli in experimental infection in vivo. Br. J. Exp. Pathol. 70:1989;697-704.
    • (1989) Br. J. Exp. Pathol. , vol.70 , pp. 697-704
    • Zagulski, T.1    Lipinski, P.2    Zagulska, A.3    Broniek, S.4    Jarzabek, Z.5
  • 55
    • 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
  • 56
    • 0018662290 scopus 로고
    • Specificity of lactoferrin as an inhibitor of granulocyte-macrophage colony-stimulating activity production from fetal mouse liver cells
    • Zucali J.R., Broxmeyer H.E., Ulatowski J.A. Specificity of lactoferrin as an inhibitor of granulocyte-macrophage colony-stimulating activity production from fetal mouse liver cells. Blood. 54:1979;951-954.
    • (1979) Blood , vol.54 , pp. 951-954
    • Zucali, J.R.1    Broxmeyer, H.E.2    Ulatowski, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.