메뉴 건너뛰기




Volumn 166, Issue 4, 2014, Pages 1839-1851

Proteolytic and N-glycan processing of human α1-antitrypsin expressed in Nicotiana benthamiana

Author keywords

[No Author keywords available]

Indexed keywords

NICOTIANA BENTHAMIANA;

EID: 84914133229     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.114.250720     Document Type: Article
Times cited : (54)

References (76)
  • 1
    • 50849113047 scopus 로고    scopus 로고
    • Expression of modified gene encoding functional human alpha-1-antitrypsin protein in transgenic tomato plants
    • Agarwal S, Singh R, Sanyal I, Amla DV (2008) Expression of modified gene encoding functional human alpha-1-antitrypsin protein in transgenic tomato plants. Transgenic Res 17: 881-896.
    • (2008) Transgenic Res , vol.17 , pp. 881-896
    • Agarwal, S.1    Singh, R.2    Sanyal, I.3    Amla, D.V.4
  • 3
    • 0034017941 scopus 로고    scopus 로고
    • Should health-care systems pay for replacement therapy in patients with alpha(1)-antitrypsin deficiency? A critical review and cost-effectiveness analysis
    • Alkins SA, O'Malley P (2000) Should health-care systems pay for replacement therapy in patients with alpha(1)-antitrypsin deficiency? A critical review and cost-effectiveness analysis. Chest 117: 875-880.
    • (2000) Chest , vol.117 , pp. 875-880
    • Alkins, S.A.1    O'Malley, P.2
  • 4
    • 80052593806 scopus 로고    scopus 로고
    • Expression and purification of functionally active recombinant human alpha 1-antitrypsin in methylotrophic yeast Pichia pastoris
    • Arjmand S, Bidram E, Lotfi AS, Shamsara M, Mowla SJ (2011) Expression and purification of functionally active recombinant human alpha 1-antitrypsin in methylotrophic yeast Pichia pastoris. Avicenna J Med Biotechnol 3: 127-134.
    • (2011) Avicenna J Med Biotechnol , vol.3 , pp. 127-134
    • Arjmand, S.1    Bidram, E.2    Lotfi, A.S.3    Shamsara, M.4    Mowla, S.J.5
  • 6
    • 0028045033 scopus 로고
    • Clinical features and molecular characteristics of alpha 1-antitrypsin deficiency
    • Blank CA, Brantly M (1994) Clinical features and molecular characteristics of alpha 1-antitrypsin deficiency. Ann Allergy 72: 105-120.
    • (1994) Ann Allergy , vol.72 , pp. 105-120
    • Blank, C.A.1    Brantly, M.2
  • 13
    • 84866037634 scopus 로고    scopus 로고
    • Glyco-engineering in plants to produce human-like N-glycan structures
    • Castilho A, Steinkellner H (2012) Glyco-engineering in plants to produce human-like N-glycan structures. Biotechnol J 7: 1088-1098.
    • (2012) Biotechnol J , vol.7 , pp. 1088-1098
    • Castilho, A.1    Steinkellner, H.2
  • 17
    • 0034831423 scopus 로고    scopus 로고
    • Secretion of biologically active glycoforms of bovine follicle stimulating hormone in plants
    • Dirnberger D, Steinkellner H, Abdennebi L, Remy JJ, van de Wiel D (2001) Secretion of biologically active glycoforms of bovine follicle stimulating hormone in plants. Eur J Biochem 268: 4570-4579.
    • (2001) Eur J Biochem , vol.268 , pp. 4570-4579
    • Dirnberger, D.1    Steinkellner, H.2    Abdennebi, L.3    Remy, J.J.4    van de Wiel, D.5
  • 18
    • 33747141725 scopus 로고    scopus 로고
    • Foreign protein degradation and instability in plants and plant tissue cultures
    • Doran PM (2006) Foreign protein degradation and instability in plants and plant tissue cultures. Trends Biotechnol 24: 426-432.
    • (2006) Trends Biotechnol , vol.24 , pp. 426-432
    • Doran, P.M.1
  • 22
  • 23
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins PG (2002) Serpin structure, mechanism, and function. Chem Rev 102: 4751-4804.
    • (2002) Chem Rev , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 26
    • 83055194481 scopus 로고    scopus 로고
    • A protease activity-depleted environment for heterologous proteins migrating towards the leaf cell apoplast
    • Goulet C, Khalf M, Sainsbury F, D'Aoust MA, Michaud D (2012) A protease activity-depleted environment for heterologous proteins migrating towards the leaf cell apoplast. Plant Biotechnol J 10: 83-94.
    • (2012) Plant Biotechnol J , vol.10 , pp. 83-94
    • Goulet, C.1    Khalf, M.2    Sainsbury, F.3    D'Aoust, M.A.4    Michaud, D.5
  • 27
    • 84899630021 scopus 로고    scopus 로고
    • Taliglucerase alfa: An enzyme replacement therapy using plant cell expression technology
    • Grabowski GA, Golembo M, Shaaltiel Y (2014) Taliglucerase alfa: an enzyme replacement therapy using plant cell expression technology. Mol Genet Metab 112: 1-8.
    • (2014) Mol Genet Metab , vol.112 , pp. 1-8
    • Grabowski, G.A.1    Golembo, M.2    Shaaltiel, Y.3
  • 29
    • 79956222624 scopus 로고    scopus 로고
    • Chaperones and foldases in endoplasmic reticulum stress signaling in plants
    • Gupta D, Tuteja N (2011) Chaperones and foldases in endoplasmic reticulum stress signaling in plants. Plant Signal Behav 6: 232-236.
    • (2011) Plant Signal Behav , vol.6 , pp. 232-236
    • Gupta, D.1    Tuteja, N.2
  • 33
    • 58249094041 scopus 로고    scopus 로고
    • Bioreactor strategies for improving production yield and functionality of a recombinant human protein in transgenic tobacco cell cultures
    • Huang TK, Plesha MA, Falk BW, Dandekar AM, McDonald KA (2009) Bioreactor strategies for improving production yield and functionality of a recombinant human protein in transgenic tobacco cell cultures. Biotechnol Bioeng 102: 508-520.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 508-520
    • Huang, T.K.1    Plesha, M.A.2    Falk, B.W.3    Dandekar, A.M.4    McDonald, K.A.5
  • 34
    • 77953592097 scopus 로고    scopus 로고
    • Semicontinuous bioreactor production of a recombinant human therapeutic protein using a chemically inducible viral amplicon expression system in transgenic plant cell suspension cultures
    • Huang TK, Plesha MA, McDonald KA (2010) Semicontinuous bioreactor production of a recombinant human therapeutic protein using a chemically inducible viral amplicon expression system in transgenic plant cell suspension cultures. Biotechnol Bioeng 106: 408-421.
    • (2010) Biotechnol Bioeng , vol.106 , pp. 408-421
    • Huang, T.K.1    Plesha, M.A.2    McDonald, K.A.3
  • 35
    • 84865320813 scopus 로고    scopus 로고
    • Differential subcellular targeting of recombinant human a1-proteinase inhibitor influences yield, biological activity and in planta stability of the protein in transgenic tomato plants
    • Jha S, Agarwal S, Sanyal I, Jain GK, Amla DV (2012) Differential subcellular targeting of recombinant human a1-proteinase inhibitor influences yield, biological activity and in planta stability of the protein in transgenic tomato plants. Plant Sci 196: 53-66.
    • (2012) Plant Sci , vol.196 , pp. 53-66
    • Jha, S.1    Agarwal, S.2    Sanyal, I.3    Jain, G.K.4    Amla, D.V.5
  • 36
    • 0018276853 scopus 로고
    • Structural evidence for methionine at the reactive site of human alpha-1-proteinase inhibitor
    • Johnson D, Travis J (1978) Structural evidence for methionine at the reactive site of human alpha-1-proteinase inhibitor. J Biol Chem 253: 7142-7144.
    • (1978) J Biol Chem , vol.253 , pp. 7142-7144
    • Johnson, D.1    Travis, J.2
  • 37
    • 0022843745 scopus 로고
    • Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region
    • Johnson DA, Barrett AJ, Mason RW (1986) Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region. J Biol Chem 261: 14748-14751.
    • (1986) J Biol Chem , vol.261 , pp. 14748-14751
    • Johnson, D.A.1    Barrett, A.J.2    Mason, R.W.3
  • 38
    • 33745065087 scopus 로고    scopus 로고
    • Recombinant human alpha-1 proteinase inhibitor: Towards therapeutic use
    • Karnaukhova E, Ophir Y, Golding B (2006) Recombinant human alpha-1 proteinase inhibitor: towards therapeutic use. Amino Acids 30: 317-332.
    • (2006) Amino Acids , vol.30 , pp. 317-332
    • Karnaukhova, E.1    Ophir, Y.2    Golding, B.3
  • 40
    • 33645100367 scopus 로고    scopus 로고
    • Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms
    • Kolarich D, Weber A, Turecek PL, Schwarz HP, Altmann F (2006) Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms. Proteomics 6: 3369-3380.
    • (2006) Proteomics , vol.6 , pp. 3369-3380
    • Kolarich, D.1    Weber, A.2    Turecek, P.L.3    Schwarz, H.P.4    Altmann, F.5
  • 43
    • 79953221436 scopus 로고    scopus 로고
    • Beta-N-acetylhexosaminidases HEXO1 and HEXO3 are responsible for the formation of paucimannosidic N-glycans in Arabidopsis thaliana
    • Liebminger E, Veit C, Pabst M, Batoux M, Zipfel C, Altmann F, Mach L, Strasser R (2011) Beta-N-acetylhexosaminidases HEXO1 and HEXO3 are responsible for the formation of paucimannosidic N-glycans in Arabidopsis thaliana. J Biol Chem 286: 10793-10802.
    • (2011) J Biol Chem , vol.286 , pp. 10793-10802
    • Liebminger, E.1    Veit, C.2    Pabst, M.3    Batoux, M.4    Zipfel, C.5    Altmann, F.6    Mach, L.7    Strasser, R.8
  • 46
    • 79953683705 scopus 로고    scopus 로고
    • Expression of antibody fragments with a controlled N-glycosylation pattern and induction of endoplasmic reticulum-derived vesicles in seeds of Arabidopsis
    • Loos A, Van Droogenbroeck B, Hillmer S, Grass J, Pabst M, Castilho A, Kunert R, Liang M, Arcalis E, Robinson DG, et al (2011) Expression of antibody fragments with a controlled N-glycosylation pattern and induction of endoplasmic reticulum-derived vesicles in seeds of Arabidopsis. Plant Physiol 155: 2036-2048.
    • (2011) Plant Physiol , vol.155 , pp. 2036-2048
    • Loos, A.1    Van Droogenbroeck, B.2    Hillmer, S.3    Grass, J.4    Pabst, M.5    Castilho, A.6    Kunert, R.7    Liang, M.8    Arcalis, E.9    Robinson, D.G.10
  • 47
    • 84879725035 scopus 로고    scopus 로고
    • Development and analysis of alpha 1-antitrypsin neoglycoproteins: The impact of additional N-glycosylation sites on serum half-life
    • Lusch A, Kaup M, Marx U, Tauber R, Blanchard V, Berger M (2013) Development and analysis of alpha 1-antitrypsin neoglycoproteins: the impact of additional N-glycosylation sites on serum half-life. Mol Pharm 10: 2616-2629.
    • (2013) Mol Pharm , vol.10 , pp. 2616-2629
    • Lusch, A.1    Kaup, M.2    Marx, U.3    Tauber, R.4    Blanchard, V.5    Berger, M.6
  • 48
    • 2342525801 scopus 로고    scopus 로고
    • In planta engineering of viral RNA replicons: Efficient assembly by recombination of DNA modules delivered by Agrobacterium
    • Marillonnet S, Giritch A, Gils M, Kandzia R, Klimyuk V, Gleba Y (2004) In planta engineering of viral RNA replicons: efficient assembly by recombination of DNA modules delivered by Agrobacterium. Proc Natl Acad Sci USA 101: 6852-6857.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6852-6857
    • Marillonnet, S.1    Giritch, A.2    Gils, M.3    Kandzia, R.4    Klimyuk, V.5    Gleba, Y.6
  • 49
    • 24944498904 scopus 로고    scopus 로고
    • Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants
    • Marillonnet S, Thoeringer C, Kandzia R, Klimyuk V, Gleba Y (2005) Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants. Nat Biotechnol 23: 718-723.
    • (2005) Nat Biotechnol , vol.23 , pp. 718-723
    • Marillonnet, S.1    Thoeringer, C.2    Kandzia, R.3    Klimyuk, V.4    Gleba, Y.5
  • 50
    • 0025828198 scopus 로고
    • Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinasecomplexed, and reactive site cleaved serpins: Comparison of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, antithrombin III, alpha 2-antiplasmin, angiotensinogen, and ovalbumin
    • Mast AE, Enghild JJ, Pizzo SV, Salvesen G (1991) Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinasecomplexed, and reactive site cleaved serpins: comparison of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, antithrombin III, alpha 2-antiplasmin, angiotensinogen, and ovalbumin. Biochemistry 30: 1723-1730.
    • (1991) Biochemistry , vol.30 , pp. 1723-1730
    • Mast, A.E.1    Enghild, J.J.2    Pizzo, S.V.3    Salvesen, G.4
  • 51
    • 20144367975 scopus 로고    scopus 로고
    • Production of human alpha-1-antitrypsin from transgenic rice cell culture in a membrane bioreactor
    • McDonald KA, Hong LM, Trombly DM, Xie Q, Jackman AP (2005) Production of human alpha-1-antitrypsin from transgenic rice cell culture in a membrane bioreactor. Biotechnol Prog 21: 728-734.
    • (2005) Biotechnol Prog , vol.21 , pp. 728-734
    • McDonald, K.A.1    Hong, L.M.2    Trombly, D.M.3    Xie, Q.4    Jackman, A.P.5
  • 52
    • 62149100748 scopus 로고    scopus 로고
    • High-level expression of active human alpha1-antitrypsin in transgenic tobacco chloroplasts
    • Nadai M, Bally J, Vitel M, Job C, Tissot G, Botterman J, Dubald M (2009) High-level expression of active human alpha1-antitrypsin in transgenic tobacco chloroplasts. Transgenic Res 18: 173-183.
    • (2009) Transgenic Res , vol.18 , pp. 173-183
    • Nadai, M.1    Bally, J.2    Vitel, M.3    Job, C.4    Tissot, G.5    Botterman, J.6    Dubald, M.7
  • 53
    • 84864365553 scopus 로고    scopus 로고
    • Function and 3D structure of the N-glycans on glycoproteins
    • Nagae M, Yamaguchi Y (2012) Function and 3D structure of the N-glycans on glycoproteins. Int J Mol Sci 13: 8398-8429.
    • (2012) Int J Mol Sci , vol.13 , pp. 8398-8429
    • Nagae, M.1    Yamaguchi, Y.2
  • 54
    • 0033617197 scopus 로고    scopus 로고
    • Purification and characterization of a novel cysteine proteinase (periodontain) from Porphyromonas gingivalis. Evidence for a role in the inactivation of human alpha1-proteinase inhibitor
    • Nelson D, Potempa J, Kordula T, Travis J (1999) Purification and characterization of a novel cysteine proteinase (periodontain) from Porphyromonas gingivalis. Evidence for a role in the inactivation of human alpha1-proteinase inhibitor. J Biol Chem 274: 12245-12251.
    • (1999) J Biol Chem , vol.274 , pp. 12245-12251
    • Nelson, D.1    Potempa, J.2    Kordula, T.3    Travis, J.4
  • 55
    • 0032113805 scopus 로고    scopus 로고
    • Inactivation of alpha1-proteinase inhibitor as a broad screen for detecting proteolytic activities in unknown samples
    • Nelson D, Potempa J, Travis J (1998) Inactivation of alpha1-proteinase inhibitor as a broad screen for detecting proteolytic activities in unknown samples. Anal Biochem 260: 230-236.
    • (1998) Anal Biochem , vol.260 , pp. 230-236
    • Nelson, D.1    Potempa, J.2    Travis, J.3
  • 56
    • 84897105776 scopus 로고    scopus 로고
    • The human anti-HIV antibodies 2F5, 2G12, and PG9 differ in their susceptibility to proteolytic degradation: Down-regulation of endogenous serine and cysteine proteinase activities could improve antibody production in plant-based expression platforms
    • Niemer M, Mehofer U, Torres Acosta JA, Verdianz M, Henkel T, Loos A, Strasser R, Maresch D, Rademacher T, Steinkellner H, et al (2014) The human anti-HIV antibodies 2F5, 2G12, and PG9 differ in their susceptibility to proteolytic degradation: down-regulation of endogenous serine and cysteine proteinase activities could improve antibody production in plant-based expression platforms. Biotechnol J 9: 493-500.
    • (2014) Biotechnol J , vol.9 , pp. 493-500
    • Niemer, M.1    Mehofer, U.2    Torres Acosta, J.A.3    Verdianz, M.4    Henkel, T.5    Loos, A.6    Strasser, R.7    Maresch, D.8    Rademacher, T.9    Steinkellner, H.10
  • 57
    • 84867774199 scopus 로고    scopus 로고
    • Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140
    • Pabst M, Chang M, Stadlmann J, Altmann F (2012) Glycan profiles of the 27 N-glycosylation sites of the HIV envelope protein CN54gp140. Biol Chem 393: 719-730.
    • (2012) Biol Chem , vol.393 , pp. 719-730
    • Pabst, M.1    Chang, M.2    Stadlmann, J.3    Altmann, F.4
  • 59
    • 84878006295 scopus 로고    scopus 로고
    • The design of a new truncated and engineered alpha1-antitrypsin based on theoretical studies: An antiprotease therapeutics for pulmonary diseases
    • Pirooznia N, Hasannia S, Arab SS, Lotfi AS, Ghanei M, Shali A (2013) The design of a new truncated and engineered alpha1-antitrypsin based on theoretical studies: an antiprotease therapeutics for pulmonary diseases. Theor Biol Med Model 10: 36.
    • (2013) Theor Biol Med Model , vol.10 , pp. 36
    • Pirooznia, N.1    Hasannia, S.2    Arab, S.S.3    Lotfi, A.S.4    Ghanei, M.5    Shali, A.6
  • 60
    • 37149026984 scopus 로고    scopus 로고
    • High-level transient production of a heterologous protein in plants by optimizing induction of a chemically inducible viral amplicon expression system
    • Plesha MA, Huang TK, Dandekar AM, Falk BW, McDonald KA (2007) High-level transient production of a heterologous protein in plants by optimizing induction of a chemically inducible viral amplicon expression system. Biotechnol Prog 23: 1277-1285.
    • (2007) Biotechnol Prog , vol.23 , pp. 1277-1285
    • Plesha, M.A.1    Huang, T.K.2    Dandekar, A.M.3    Falk, B.W.4    McDonald, K.A.5
  • 61
    • 0023031993 scopus 로고
    • The inactivation of human plasma alpha 1-proteinase inhibitor by proteinases from Staphylococcus aureus
    • Potempa J, Watorek W, Travis J (1986) The inactivation of human plasma alpha 1-proteinase inhibitor by proteinases from Staphylococcus aureus. J Biol Chem 261: 14330-14334.
    • (1986) J Biol Chem , vol.261 , pp. 14330-14334
    • Potempa, J.1    Watorek, W.2    Travis, J.3
  • 64
    • 84897094860 scopus 로고    scopus 로고
    • Expression of human butyrylcholinesterase with an engineered glycosylation profile resembling the plasma-derived orthologue
    • Schneider JD, Castilho A, Neumann L, Altmann F, Loos A, Kannan L, Mor TS, Steinkellner H (2014a) Expression of human butyrylcholinesterase with an engineered glycosylation profile resembling the plasma-derived orthologue. Biotechnol J 9: 501-510.
    • (2014) Biotechnol J , vol.9 , pp. 501-510
    • Schneider, J.D.1    Castilho, A.2    Neumann, L.3    Altmann, F.4    Loos, A.5    Kannan, L.6    Mor, T.S.7    Steinkellner, H.8
  • 66
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer J, Vavra U, Stadlmann J, Hawes C, Mach L, Steinkellner H, Strasser R (2009) Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic 10: 101-115.
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1    Vavra, U.2    Stadlmann, J.3    Hawes, C.4    Mach, L.5    Steinkellner, H.6    Strasser, R.7
  • 67
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
    • Stadlmann J, Pabst M, Kolarich D, Kunert R, Altmann F (2008) Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides. Proteomics 8: 2858-2871.
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3    Kunert, R.4    Altmann, F.5
  • 73
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis J, Salvesen GS (1983) Human plasma proteinase inhibitors. Annu Rev Biochem 52: 655-709.
    • (1983) Annu Rev Biochem , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 74
    • 0035988092 scopus 로고    scopus 로고
    • Bioreactor production of human alpha(1)-antitrypsin using metabolically regulated plant cell cultures
    • Trexler MM, McDonald KA, Jackman AP (2002) Bioreactor production of human alpha(1)-antitrypsin using metabolically regulated plant cell cultures. Biotechnol Prog 18: 501-508.
    • (2002) Biotechnol Prog , vol.18 , pp. 501-508
    • Trexler, M.M.1    McDonald, K.A.2    Jackman, A.P.3
  • 75
    • 44949258132 scopus 로고    scopus 로고
    • Plant proteases: From phenotypes to molecular mechanisms
    • van der Hoorn RA (2008) Plant proteases: from phenotypes to molecular mechanisms. Annu Rev Plant Biol 59: 191-223.
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 191-223
    • van der Hoorn, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.