메뉴 건너뛰기




Volumn 168, Issue 4, 2013, Pages 666-675

Novel recombinant human lactoferrin: Differential activation of oxidative stress related gene expression

Author keywords

Antioxidant; Gene expression; Inflammation; Recombinant human lactoferrin

Indexed keywords

BIOLOGICAL PROPERTIES; CATION EXCHANGE CHROMATOGRAPHY; CHINESE HAMSTER OVARY CELLS; INFLAMMATION; MALDI-TOF MASS SPECTROMETRIC ANALYSIS; POST-TRANSLATIONAL MODIFICATIONS; RECOMBINANT HUMAN LACTOFERRIN; RECOMBINANT HUMAN LACTOFERRIN (RHLF);

EID: 84888847586     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.09.011     Document Type: Article
Times cited : (58)

References (59)
  • 3
    • 0032893748 scopus 로고    scopus 로고
    • Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process
    • Baveye S., Elass E., Mazurier J., Spik G., Legrand D. Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process. Clin. Chem. Lab. Med. 1999, 37:281-286.
    • (1999) Clin. Chem. Lab. Med. , vol.37 , pp. 281-286
    • Baveye, S.1    Elass, E.2    Mazurier, J.3    Spik, G.4    Legrand, D.5
  • 4
    • 0028618679 scopus 로고
    • Lactoferrin and the inflammatory response
    • Baynes R.D., Bezwoda W.R. Lactoferrin and the inflammatory response. Adv. Exp. Med. Biol. 1994, 357:133-141.
    • (1994) Adv. Exp. Med. Biol. , vol.357 , pp. 133-141
    • Baynes, R.D.1    Bezwoda, W.R.2
  • 8
    • 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. 1978, 72:248-254.
    • (1978) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 33745726019 scopus 로고    scopus 로고
    • Oxidative stress disrupts internalization and endocytic trafficking of transferrin in a human malignant keratinocyte line
    • Cheng J., Vieira A. Oxidative stress disrupts internalization and endocytic trafficking of transferrin in a human malignant keratinocyte line. Cell Biochem. Biophys. 2006, 45:177-184.
    • (2006) Cell Biochem. Biophys. , vol.45 , pp. 177-184
    • Cheng, J.1    Vieira, A.2
  • 12
    • 77957019333 scopus 로고    scopus 로고
    • Recombinant human lactoferrin: a valuable protein for pharmaceutical products and functional foods
    • Conesa C., Calvo M., Sánchez L. Recombinant human lactoferrin: a valuable protein for pharmaceutical products and functional foods. Biotechnol. Adv. 2010, 28:831-838.
    • (2010) Biotechnol. Adv. , vol.28 , pp. 831-838
    • Conesa, C.1    Calvo, M.2    Sánchez, L.3
  • 13
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis
    • D'Autréaux B., Toledano M.B. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat. Rev. Mol. Cell Biol. 2007, 8:813-824.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 813-824
    • D'Autréaux, B.1    Toledano, M.B.2
  • 14
    • 57349105745 scopus 로고    scopus 로고
    • Whole-blood culture is a valid low-cost method to measure monocytic cytokines - a comparison of cytokine production in cultures of human whole-blood, mononuclear cells and monocytes
    • Damsgaard C.T., Lauritzen L., Calder P.C., Kjaer T.M., Frøkiaer H. Whole-blood culture is a valid low-cost method to measure monocytic cytokines - a comparison of cytokine production in cultures of human whole-blood, mononuclear cells and monocytes. J. Immunol. Methods 2009, 340:95-101.
    • (2009) J. Immunol. Methods , vol.340 , pp. 95-101
    • Damsgaard, C.T.1    Lauritzen, L.2    Calder, P.C.3    Kjaer, T.M.4    Frøkiaer, H.5
  • 15
    • 0035921175 scopus 로고    scopus 로고
    • Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII
    • Davies J., Jiang L., Pan L.Z., LaBarre M.J., Anderson D., Reff M. Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII. Biotechnol. Bioeng. 2001, 74:288-294.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 288-294
    • Davies, J.1    Jiang, L.2    Pan, L.Z.3    LaBarre, M.J.4    Anderson, D.5    Reff, M.6
  • 16
    • 71049170514 scopus 로고    scopus 로고
    • Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry
    • Ding W., Nothaft H., Szymanski C.M., Kelly J. Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry. Mol. Cell. Proteomics 2009, 8:2170-2185.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2170-2185
    • Ding, W.1    Nothaft, H.2    Szymanski, C.M.3    Kelly, J.4
  • 18
    • 25844442417 scopus 로고    scopus 로고
    • Altered glycan structures: the molecular basis of congenital disorders of glycosylation
    • Freeze H.H., Aebi M. Altered glycan structures: the molecular basis of congenital disorders of glycosylation. Curr. Opin. Struct. Biol. 2005, 15:490-498.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 490-498
    • Freeze, H.H.1    Aebi, M.2
  • 19
    • 0024497455 scopus 로고
    • Survival of recombinant erythropoietin in the circulation: the role of carbohydrates
    • Fukuda M.N., Sasaki H., Lopez L., Fukuda M. Survival of recombinant erythropoietin in the circulation: the role of carbohydrates. Blood 1989, 73:84-89.
    • (1989) Blood , vol.73 , pp. 84-89
    • Fukuda, M.N.1    Sasaki, H.2    Lopez, L.3    Fukuda, M.4
  • 22
    • 0037365579 scopus 로고    scopus 로고
    • Altered glycosylation of alpha1-acid glycoprotein in patients with inflammation and diabetes mellitus
    • Higai K., Azuma Y., Aoki Y., Matsumoto K. Altered glycosylation of alpha1-acid glycoprotein in patients with inflammation and diabetes mellitus. Clin. Chim. Acta 2003, 329:117-125.
    • (2003) Clin. Chim. Acta , vol.329 , pp. 117-125
    • Higai, K.1    Azuma, Y.2    Aoki, Y.3    Matsumoto, K.4
  • 23
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler P., Khattak S.F., Li Z.J. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 2009, 19:936-949.
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 24
    • 0025488009 scopus 로고
    • Role of breast-feeding in the prevention and treatment of diarrhoea
    • Huffman S.L., Combest C. Role of breast-feeding in the prevention and treatment of diarrhoea. J. Diarrhoeal Dis. Res. 1990, 8:68-81.
    • (1990) J. Diarrhoeal Dis. Res. , vol.8 , pp. 68-81
    • Huffman, S.L.1    Combest, C.2
  • 25
    • 15944378224 scopus 로고    scopus 로고
    • Lactoferrin augments BCG vaccine efficacy to generate T helper response and subsequent protection against challenge with virulent Mycobacterium tuberculosis
    • Hwang S.A., Kruzel M.L., Actor J.K. Lactoferrin augments BCG vaccine efficacy to generate T helper response and subsequent protection against challenge with virulent Mycobacterium tuberculosis. Int. Immunopharmacol. 2005, 5:591-599.
    • (2005) Int. Immunopharmacol. , vol.5 , pp. 591-599
    • Hwang, S.A.1    Kruzel, M.L.2    Actor, J.K.3
  • 26
    • 34548248672 scopus 로고    scopus 로고
    • Lactoferrin enhanced efficacy of the BCG vaccine to generate host protective responses against challenge with virulent Mycobacterium tuberculosis
    • Hwang S.A., Wilk K.M., Budnicka M., Olsen M., Bangale Y.A., Hunter R.L., Kruzel M.L., Actor J.K. Lactoferrin enhanced efficacy of the BCG vaccine to generate host protective responses against challenge with virulent Mycobacterium tuberculosis. Vaccine 2007, 25:6730-6743.
    • (2007) Vaccine , vol.25 , pp. 6730-6743
    • Hwang, S.A.1    Wilk, K.M.2    Budnicka, M.3    Olsen, M.4    Bangale, Y.A.5    Hunter, R.L.6    Kruzel, M.L.7    Actor, J.K.8
  • 27
    • 67349256155 scopus 로고    scopus 로고
    • A novel recombinant human lactoferrin augments the BCG vaccine and protects alveolar integrity upon infection with Mycobacterium tuberculosis in mice
    • Hwang S.A., Wilk K., Kruzel M.L., Actor J.K. A novel recombinant human lactoferrin augments the BCG vaccine and protects alveolar integrity upon infection with Mycobacterium tuberculosis in mice. Vaccine 2009, 27(23):3026-3034.
    • (2009) Vaccine , vol.27 , Issue.23 , pp. 3026-3034
    • Hwang, S.A.1    Wilk, K.2    Kruzel, M.L.3    Actor, J.K.4
  • 30
    • 77952395053 scopus 로고    scopus 로고
    • Lactoferrin decreases LPS-induced mitochondrial dysfunction in cultured cells and in animal endotoxemia model
    • Kruzel M.L., Actor J.K., Radak Z., Bacsi A., Saavedra-Molina A., Boldogh I. Lactoferrin decreases LPS-induced mitochondrial dysfunction in cultured cells and in animal endotoxemia model. Innate Immun. 2010, 16:67-79.
    • (2010) Innate Immun. , vol.16 , pp. 67-79
    • Kruzel, M.L.1    Actor, J.K.2    Radak, Z.3    Bacsi, A.4    Saavedra-Molina, A.5    Boldogh, I.6
  • 31
    • 33748751668 scopus 로고    scopus 로고
    • Lactoferrin decreases pollen antigen-induced allergic airway inflammation in a murine model of asthma
    • Kruzel M.L., Bacsi A., Choudhury B., Sur S., Boldogh I. Lactoferrin decreases pollen antigen-induced allergic airway inflammation in a murine model of asthma. Immunology 2006, 119:159-166.
    • (2006) Immunology , vol.119 , pp. 159-166
    • Kruzel, M.L.1    Bacsi, A.2    Choudhury, B.3    Sur, S.4    Boldogh, I.5
  • 32
    • 0036379733 scopus 로고    scopus 로고
    • Differential effects of prophylactic, concurrent and therapeutic lactoferrin treatment on LPS-induced inflammatory responses in mice
    • Kruzel M.L., Harari Y., Mailman D., Actor J.K., Zimecki M. Differential effects of prophylactic, concurrent and therapeutic lactoferrin treatment on LPS-induced inflammatory responses in mice. Clin. Exp. Immunol. 2002, 130:25-31.
    • (2002) Clin. Exp. Immunol. , vol.130 , pp. 25-31
    • Kruzel, M.L.1    Harari, Y.2    Mailman, D.3    Actor, J.K.4    Zimecki, M.5
  • 33
    • 70449732650 scopus 로고    scopus 로고
    • Pharmacological significance of glycosylation in therapeutic proteins
    • Li H., d'Anjou M. Pharmacological significance of glycosylation in therapeutic proteins. Curr. Opin. Biotechnol. 2009, 20:678-684.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 678-684
    • Li, H.1    d'Anjou, M.2
  • 35
    • 0029130333 scopus 로고
    • Lactoferrin: molecular structure and biological function
    • Lönnerdal B., Iyer S. Lactoferrin: molecular structure and biological function. Annu. Rev. Nutr. 1995, 15:93-110.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 93-110
    • Lönnerdal, B.1    Iyer, S.2
  • 36
  • 40
    • 54949106904 scopus 로고    scopus 로고
    • Mammalian glycosylation in immunity
    • Marth J.D., Grewal P.K. Mammalian glycosylation in immunity. Nat. Rev. Immunol. 2008, 8:874-887.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 874-887
    • Marth, J.D.1    Grewal, P.K.2
  • 41
    • 0033782205 scopus 로고    scopus 로고
    • Autoantibody activity of IgG rheumatoid factor increases with decreasing levels of galactosylation and sialylation
    • Matsumoto A., Shikata K., Takeuchi F., Kojima N., Mizuochi T. Autoantibody activity of IgG rheumatoid factor increases with decreasing levels of galactosylation and sialylation. J. Biochem. 2000, 128:621-628.
    • (2000) J. Biochem. , vol.128 , pp. 621-628
    • Matsumoto, A.1    Shikata, K.2    Takeuchi, F.3    Kojima, N.4    Mizuochi, T.5
  • 42
    • 79959438755 scopus 로고    scopus 로고
    • Serine protease PrtA from Streptococcus pneumoniae plays a role in the killing of S. pneumoniae by apolactoferrin
    • Mirza S., Wilson L., Benjamin W.H., Novak J., Barnes S., Hollingshead S.K., Briles D.E. Serine protease PrtA from Streptococcus pneumoniae plays a role in the killing of S. pneumoniae by apolactoferrin. Infect. Immun. 2011, 79:2440-2450.
    • (2011) Infect. Immun. , vol.79 , pp. 2440-2450
    • Mirza, S.1    Wilson, L.2    Benjamin, W.H.3    Novak, J.4    Barnes, S.5    Hollingshead, S.K.6    Briles, D.E.7
  • 43
    • 0022416851 scopus 로고
    • Comparison of human lactoferrins from milk and neutrophilic leucocytes. Relative molecular mass, isoelectric point, iron-binding properties and uptake by the liver
    • Moguilevsky N., Retegui L.A., Masson P.L. Comparison of human lactoferrins from milk and neutrophilic leucocytes. Relative molecular mass, isoelectric point, iron-binding properties and uptake by the liver. Biochem. J. 1985, 229:353-359.
    • (1985) Biochem. J. , vol.229 , pp. 353-359
    • Moguilevsky, N.1    Retegui, L.A.2    Masson, P.L.3
  • 45
    • 66149149459 scopus 로고    scopus 로고
    • Analysis of N- and O-linked glycans from glycoproteins using MALDI-TOF mass spectrometry
    • Morelle W., Faid V., Chirat F., Michalski J.C. Analysis of N- and O-linked glycans from glycoproteins using MALDI-TOF mass spectrometry. Methods Mol. Biol. 2009, 534:5-21.
    • (2009) Methods Mol. Biol. , vol.534 , pp. 5-21
    • Morelle, W.1    Faid, V.2    Chirat, F.3    Michalski, J.C.4
  • 47
    • 58149121478 scopus 로고    scopus 로고
    • Effect of lactoferrin on enteric pathogens
    • Ochoa T.J., Cleary T.G. Effect of lactoferrin on enteric pathogens. Biochimie 2009, 91:30-34.
    • (2009) Biochimie , vol.91 , pp. 30-34
    • Ochoa, T.J.1    Cleary, T.G.2
  • 48
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K., Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell 2006, 126:855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 51
    • 70349886556 scopus 로고    scopus 로고
    • Folding of glycoproteins: toward understanding the biophysics of the glycosylation code
    • Shental-Bechor D., Levy Y. Folding of glycoproteins: toward understanding the biophysics of the glycosylation code. Curr. Opin. Struct. Biol. 2009, 19:524-533.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 524-533
    • Shental-Bechor, D.1    Levy, Y.2
  • 52
    • 25444435396 scopus 로고    scopus 로고
    • Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins
    • Sinclair A.M., Elliott S. Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J. Pharm. Sci. 2005, 94:1626-1635.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1626-1635
    • Sinclair, A.M.1    Elliott, S.2
  • 53
    • 0024119835 scopus 로고
    • Comparative study of the primary structures of sero-, lacto- and ovotransferrin glycans from different species
    • Spik G., Coddeville B., Montreuil J. Comparative study of the primary structures of sero-, lacto- and ovotransferrin glycans from different species. Biochimie 1988, 70:1459-1469.
    • (1988) Biochimie , vol.70 , pp. 1459-1469
    • Spik, G.1    Coddeville, B.2    Montreuil, J.3
  • 55
    • 34248641665 scopus 로고    scopus 로고
    • A structural comparison of human serum transferrin and human lactoferrin
    • Wally J., Buchanan S.K. A structural comparison of human serum transferrin and human lactoferrin. Biometals 2007, 20(3-4):249-262.
    • (2007) Biometals , vol.20 , Issue.3-4 , pp. 249-262
    • Wally, J.1    Buchanan, S.K.2
  • 57
    • 4644245850 scopus 로고    scopus 로고
    • Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity
    • Yamane-Ohnuki N., Kinoshita S., Inoue-Urakubo M., Kusunoki M., Iida S., Nakano R., Wakitani M., Niwa R., Sakurada M., Uchida K., et al. Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnol. Bioeng. 2004, 87:614-622.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 614-622
    • Yamane-Ohnuki, N.1    Kinoshita, S.2    Inoue-Urakubo, M.3    Kusunoki, M.4    Iida, S.5    Nakano, R.6    Wakitani, M.7    Niwa, R.8    Sakurada, M.9    Uchida, K.10
  • 58
    • 0029810761 scopus 로고    scopus 로고
    • Heterogeneity in utilization of N-glycosylation sites Asn624 and Asn138 in human lactoferrin: a study with glycosylation-site mutants
    • van Berkel P.H., van Veen H.A., Geerts M.E., de Boer H.A., Nuijens J.H. Heterogeneity in utilization of N-glycosylation sites Asn624 and Asn138 in human lactoferrin: a study with glycosylation-site mutants. Biochem. J. 1996, 319(Pt 1):117-122.
    • (1996) Biochem. J. , vol.319 , Issue.PART 1 , pp. 117-122
    • van Berkel, P.H.1    van Veen, H.A.2    Geerts, M.E.3    de Boer, H.A.4    Nuijens, J.H.5
  • 59
    • 44049095632 scopus 로고    scopus 로고
    • Protein-glycan interactions in the control of innate and adaptive immune responses
    • van Kooyk Y., Rabinovich G.A. Protein-glycan interactions in the control of innate and adaptive immune responses. Nat. Immunol. 2008, 9:593-601.
    • (2008) Nat. Immunol. , vol.9 , pp. 593-601
    • van Kooyk, Y.1    Rabinovich, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.