메뉴 건너뛰기




Volumn 112, Issue 1, 2014, Pages 1-8

Taliglucerase alfa: An enzyme replacement therapy using plant cell expression technology

Author keywords

Acid glucosidase; Gaucher disease; Inborn errors of metabolism; Lysosomal storage disease

Indexed keywords

BETA GLUCOSIDASE; IMIGLUCERASE; MANNOSE; MANNOSE RECEPTOR; TALIGLUCERASE ALFA; VELAGLUCERASE ALFA; GLUCOSYLCERAMIDASE;

EID: 84899630021     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2014.02.011     Document Type: Review
Times cited : (112)

References (57)
  • 3
    • 0027318762 scopus 로고
    • Binding, internalization, and degradation of mannose-terminated glucocerebrosidase by macrophages
    • Sato Y., Beutler E. Binding, internalization, and degradation of mannose-terminated glucocerebrosidase by macrophages. J. Clin. Invest. 1993, 91:1909-1917.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1909-1917
    • Sato, Y.1    Beutler, E.2
  • 4
    • 0344094038 scopus 로고
    • Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages
    • Stahl P.D., Rodman J.S., Miller M.J., Schlesinger P.H. Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages. Proc. Natl. Acad. Sci. U. S. A. 1978, 75:1399-1403.
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 1399-1403
    • Stahl, P.D.1    Rodman, J.S.2    Miller, M.J.3    Schlesinger, P.H.4
  • 6
    • 0019475525 scopus 로고
    • Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation
    • Furbish F.S., Steer C.J., Krett N.L., Barranger J.A. Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation. Biochim. Biophys. Acta 1981, 673:425-434.
    • (1981) Biochim. Biophys. Acta , vol.673 , pp. 425-434
    • Furbish, F.S.1    Steer, C.J.2    Krett, N.L.3    Barranger, J.A.4
  • 8
    • 84899628378 scopus 로고    scopus 로고
    • Genzyme Corporation, Cambridge, MA
    • Cerezyme [Package Insert] 2009, Genzyme Corporation, Cambridge, MA.
    • (2009) Cerezyme [Package Insert]
  • 9
    • 84860795494 scopus 로고    scopus 로고
    • Shire Human Genetic Therapies, Inc., Cambridge, MA
    • VPRIV [Package Insert] 2010, Shire Human Genetic Therapies, Inc., Cambridge, MA.
    • (2010) VPRIV [Package Insert]
  • 10
    • 84866041577 scopus 로고    scopus 로고
    • Velaglucerase alfa in the treatment of Gaucher disease type 1
    • Burrow T.A., Grabowski G.A. Velaglucerase alfa in the treatment of Gaucher disease type 1. Clin. Investig. (Lond.) 2011, 1:285-293.
    • (2011) Clin. Investig. (Lond.) , vol.1 , pp. 285-293
    • Burrow, T.A.1    Grabowski, G.A.2
  • 11
    • 84896898592 scopus 로고    scopus 로고
    • Pfizer Labs, New York, NY
    • Elelyso [Package Insert] 2012, Pfizer Labs, New York, NY.
    • (2012) Elelyso [Package Insert]
  • 12
    • 84876576065 scopus 로고    scopus 로고
    • First plant-made biologic approved
    • Fox J.L. First plant-made biologic approved. Nat. Biotechnol. 2012, 30:472.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 472
    • Fox, J.L.1
  • 13
    • 34548110776 scopus 로고    scopus 로고
    • Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes
    • Yin J., Li G., Ren X., Herrler G. Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes. J. Biotechnol. 2007, 127:335-347.
    • (2007) J. Biotechnol. , vol.127 , pp. 335-347
    • Yin, J.1    Li, G.2    Ren, X.3    Herrler, G.4
  • 14
    • 8344236780 scopus 로고    scopus 로고
    • Plant cell cultures for the production of recombinant proteins
    • Hellwig S., Drossard J., Twyman R.M., Fischer R. Plant cell cultures for the production of recombinant proteins. Nat. Biotechnol. 2004, 22:1415-1422.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1415-1422
    • Hellwig, S.1    Drossard, J.2    Twyman, R.M.3    Fischer, R.4
  • 15
    • 42549170120 scopus 로고    scopus 로고
    • Is the drought over for pharming?
    • Kaiser J. Is the drought over for pharming?. Science 2008, 320:473-475.
    • (2008) Science , vol.320 , pp. 473-475
    • Kaiser, J.1
  • 16
    • 84897110525 scopus 로고    scopus 로고
    • Safety and immunogenicity of a plant-produced recombinant monomer hemagglutinin-based influenza vaccine derived from influenza A (H1N1)pdm09 virus: a phase 1 dose-escalation study in healthy adults
    • pii: S0264-410X(13)01381-9[Epub ahead of print] PMID: 24126211
    • Cummings J.F., Guerrero M.L., Moon J.E., Waterman P., Nielsen R.K., Jefferson S., Gross F.L., Hancock K., Katz J.M., Yusibov V. Safety and immunogenicity of a plant-produced recombinant monomer hemagglutinin-based influenza vaccine derived from influenza A (H1N1)pdm09 virus: a phase 1 dose-escalation study in healthy adults. Vaccine 2013 Oct 11, pii: S0264-410X(13)01381-9 http://dx.doi.org/10.1016/j.vaccine.2013.10.017 [Epub ahead of print] PMID: 24126211.
    • (2013) Vaccine
    • Cummings, J.F.1    Guerrero, M.L.2    Moon, J.E.3    Waterman, P.4    Nielsen, R.K.5    Jefferson, S.6    Gross, F.L.7    Hancock, K.8    Katz, J.M.9    Yusibov, V.10
  • 17
    • 77955248510 scopus 로고    scopus 로고
    • Plant-derived vaccines and other therapeutics produced in contained systems
    • Franconi R., Demurtas O.C., Massa S. Plant-derived vaccines and other therapeutics produced in contained systems. Expert Rev. Vaccines 2010, 9:877-892.
    • (2010) Expert Rev. Vaccines , vol.9 , pp. 877-892
    • Franconi, R.1    Demurtas, O.C.2    Massa, S.3
  • 18
    • 1542291118 scopus 로고    scopus 로고
    • Posttranslational modification of therapeutic proteins in plants
    • Gomord V., Faye L. Posttranslational modification of therapeutic proteins in plants. Curr. Opin. Plant Biol. 2004, 7:171-181.
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 19
    • 70449710875 scopus 로고    scopus 로고
    • Expression systems for therapeutic glycoprotein production
    • Durocher Y., Butler M. Expression systems for therapeutic glycoprotein production. Curr. Opin. Biotechnol. 2009, 20:700-707.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 700-707
    • Durocher, Y.1    Butler, M.2
  • 20
    • 84879283150 scopus 로고    scopus 로고
    • Use of baculovirus expression system for generation of virus-like particles: successes and challenges
    • Liu F., Wu X., Li L., Liu Z., Wang Z. Use of baculovirus expression system for generation of virus-like particles: successes and challenges. Protein Expr. Purif. 2013, 90:104-116.
    • (2013) Protein Expr. Purif. , vol.90 , pp. 104-116
    • Liu, F.1    Wu, X.2    Li, L.3    Liu, Z.4    Wang, Z.5
  • 24
    • 77349103873 scopus 로고    scopus 로고
    • Continued expression of plant-made vaccines following long-term cryopreservation of antigen-expressing tobacco cell cultures
    • Van Eck J., Keen P. Continued expression of plant-made vaccines following long-term cryopreservation of antigen-expressing tobacco cell cultures. In Vitro Cell. Dev. Biol. Plant 2009, 45:750-757.
    • (2009) In Vitro Cell. Dev. Biol. Plant , vol.45 , pp. 750-757
    • Van Eck, J.1    Keen, P.2
  • 28
    • 77956289133 scopus 로고    scopus 로고
    • Comparative therapeutic effects of velaglucerase alfa and imiglucerase in a Gaucher disease mouse model
    • Xu Y.H., Sun Y., Barnes S., Grabowski G.A. Comparative therapeutic effects of velaglucerase alfa and imiglucerase in a Gaucher disease mouse model. PLoS One 2010, 5:e10750.
    • (2010) PLoS One , vol.5
    • Xu, Y.H.1    Sun, Y.2    Barnes, S.3    Grabowski, G.A.4
  • 29
    • 0027179238 scopus 로고
    • Human acid beta-glucosidase. N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity
    • Berg-Fussman A., Grace M.E., Ioannou Y., Grabowski G.A. Human acid beta-glucosidase. N-glycosylation site occupancy and the effect of glycosylation on enzymatic activity. J. Biol. Chem. 1993, 268:14861-14866.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14861-14866
    • Berg-Fussman, A.1    Grace, M.E.2    Ioannou, Y.3    Grabowski, G.A.4
  • 30
    • 0029664406 scopus 로고    scopus 로고
    • Quantitative analysis of the targeting of mannose-terminal glucocerebrosidase. Predominant uptake by liver endothelial cells
    • Bijsterbosch M.K., Donker W., van de Bilt H., van Weely S., van Berkel T.J., Aerts J.M. Quantitative analysis of the targeting of mannose-terminal glucocerebrosidase. Predominant uptake by liver endothelial cells. Eur. J. Biochem. 1996, 237:344-349.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 344-349
    • Bijsterbosch, M.K.1    Donker, W.2    van de Bilt, H.3    van Weely, S.4    van Berkel, T.J.5    Aerts, J.M.6
  • 33
    • 0024542617 scopus 로고
    • Posttranslational processing of human lysosomal acid beta-glucosidase: a continuum of defects in Gaucher disease type 1 and type 2 fibroblasts
    • Bergmann J.E., Grabowski G.A. Posttranslational processing of human lysosomal acid beta-glucosidase: a continuum of defects in Gaucher disease type 1 and type 2 fibroblasts. Am. J. Hum. Genet. 1989, 44:741-750.
    • (1989) Am. J. Hum. Genet. , vol.44 , pp. 741-750
    • Bergmann, J.E.1    Grabowski, G.A.2
  • 34
    • 0028157443 scopus 로고
    • Analysis of human acid beta-glucosidase by site-directed mutagenesis and heterologous expression
    • Grace M.E., Newman K.M., Scheinker V., Berg-Fussman A., Grabowski G.A. Analysis of human acid beta-glucosidase by site-directed mutagenesis and heterologous expression. J. Biol. Chem. 1994, 269:2283-2291.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2283-2291
    • Grace, M.E.1    Newman, K.M.2    Scheinker, V.3    Berg-Fussman, A.4    Grabowski, G.A.5
  • 37
    • 0033134795 scopus 로고    scopus 로고
    • A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived beta-glucocerebrosidase: implications for clinical efficacy in treatment of Gaucher disease
    • Friedman B., Vaddi K., Preston C., Mahon E., Cataldo J.R., McPherson J.M. A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived beta-glucocerebrosidase: implications for clinical efficacy in treatment of Gaucher disease. Blood 1999, 93:2807-2816.
    • (1999) Blood , vol.93 , pp. 2807-2816
    • Friedman, B.1    Vaddi, K.2    Preston, C.3    Mahon, E.4    Cataldo, J.R.5    McPherson, J.M.6
  • 38
    • 84899632120 scopus 로고    scopus 로고
    • Enhanced in vivo uptake of glucocerebrosidase. Patent Number: 5,549,892, Genzyme Corporation, Cambridge, MA
    • B. Friedman and M. Hayes, Enhanced in vivo uptake of glucocerebrosidase. Patent Number: 5,549,892, Genzyme Corporation, Cambridge, MA 1996.
    • (1996)
    • Friedman, B.1    Hayes, M.2
  • 39
    • 0025076063 scopus 로고
    • Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I
    • Elbein A.D., Tropea J.E., Mitchell M., Kaushal G.P. Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I. J. Biol. Chem. 1990, 265:15599-15605.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15599-15605
    • Elbein, A.D.1    Tropea, J.E.2    Mitchell, M.3    Kaushal, G.P.4
  • 40
    • 33845490892 scopus 로고    scopus 로고
    • Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease
    • Brumshtein B., Wormald M.R., Silman I., Futerman A.H., Sussman J.L. Structural comparison of differently glycosylated forms of acid-beta-glucosidase, the defective enzyme in Gaucher disease. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:1458-1465.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1458-1465
    • Brumshtein, B.1    Wormald, M.R.2    Silman, I.3    Futerman, A.H.4    Sussman, J.L.5
  • 43
    • 51449092035 scopus 로고    scopus 로고
    • Wolman disease/cholesteryl ester storage disease: efficacy of plant-produced human lysosomal acid lipase in mice
    • Du H., Cameron T.L., Garger S.J., Pogue G.P., Hamm L.A., White E., Hanley K.M., Grabowski G.A. Wolman disease/cholesteryl ester storage disease: efficacy of plant-produced human lysosomal acid lipase in mice. J. Lipid Res. 2008, 49:1646-1657.
    • (2008) J. Lipid Res. , vol.49 , pp. 1646-1657
    • Du, H.1    Cameron, T.L.2    Garger, S.J.3    Pogue, G.P.4    Hamm, L.A.5    White, E.6    Hanley, K.M.7    Grabowski, G.A.8
  • 44
    • 0033805614 scopus 로고    scopus 로고
    • A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice
    • Chargelegue D., Vine N.D., van Dolleweerd C.J., Drake P.M., Ma J.K. A murine monoclonal antibody produced in transgenic plants with plant-specific glycans is not immunogenic in mice. Transgenic Res. 2000, 9:187-194.
    • (2000) Transgenic Res. , vol.9 , pp. 187-194
    • Chargelegue, D.1    Vine, N.D.2    van Dolleweerd, C.J.3    Drake, P.M.4    Ma, J.K.5
  • 45
    • 84899631321 scopus 로고    scopus 로고
    • Available at:, (Accessed: January 27, 2014) ClinicalTrials.gov, National Institutes of Health
    • ClinicalTrials.gov, National Institutes of Health Plant cell expressed recombinant human glucocerebrosidase extension trial [NCT00705939] Available at:, (Accessed: January 27, 2014). http://clinicaltrials.gov/ct2/show/NCT00705939?term=nct00705939&rank=1.
    • Plant cell expressed recombinant human glucocerebrosidase extension trial [NCT00705939]
  • 51
    • 84899657021 scopus 로고    scopus 로고
    • A multicenter, double-blind, randomized safety and efficacy study of two dose levels of taliglucerase alfa in pediatric patients with Gaucher disease [abstract 2140]
    • Zimran A., Gonzalez-Rodriguez D.E., Abrahamov A., Elstein D., Heitner R., Paz A., Brill-Almon E., Chertkoff R. A multicenter, double-blind, randomized safety and efficacy study of two dose levels of taliglucerase alfa in pediatric patients with Gaucher disease [abstract 2140]. Blood 2012, 120.
    • (2012) Blood , vol.120
    • Zimran, A.1    Gonzalez-Rodriguez, D.E.2    Abrahamov, A.3    Elstein, D.4    Heitner, R.5    Paz, A.6    Brill-Almon, E.7    Chertkoff, R.8
  • 53
    • 84880678889 scopus 로고    scopus 로고
    • The most transformative drugs of the past 25years: a survey of physicians
    • Kesselheim A.S., Avorn J. The most transformative drugs of the past 25years: a survey of physicians. Nat. Rev. Drug Discov. 2013, 12:425-431.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 425-431
    • Kesselheim, A.S.1    Avorn, J.2
  • 56
    • 77954693904 scopus 로고    scopus 로고
    • Phase 1/2 and extension study of velaglucerase alfa replacement therapy in adults with type 1 Gaucher disease: 48-month experience
    • Zimran A., Altarescu G., Philips M., Attias D., Jmoudiak M., Deeb M., Wang N., Bhirangi K., Cohn G.M., Elstein D. Phase 1/2 and extension study of velaglucerase alfa replacement therapy in adults with type 1 Gaucher disease: 48-month experience. Blood 2010, 115:4651-4656.
    • (2010) Blood , vol.115 , pp. 4651-4656
    • Zimran, A.1    Altarescu, G.2    Philips, M.3    Attias, D.4    Jmoudiak, M.5    Deeb, M.6    Wang, N.7    Bhirangi, K.8    Cohn, G.M.9    Elstein, D.10
  • 57
    • 28144437047 scopus 로고    scopus 로고
    • The role of mannosylated enzyme and the mannose receptor in enzyme replacement therapy
    • Du H., Levine M., Ganesa C., Witte D.P., Cole E.S., Grabowski G.A. The role of mannosylated enzyme and the mannose receptor in enzyme replacement therapy. Am. J. Hum. Genet. 2005, 77:1061-1074.
    • (2005) Am. J. Hum. Genet. , vol.77 , pp. 1061-1074
    • Du, H.1    Levine, M.2    Ganesa, C.3    Witte, D.P.4    Cole, E.S.5    Grabowski, G.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.