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Volumn 73, Issue 15, 2007, Pages 4805-4812

Production of recombinant β-hexosaminidase A, a potential enzyme for replacement therapy for Tay-Sachs and Sandhoff diseases, in the methylotrophic yeast Ogataea minuta

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME REPLACEMENT THERAPY (ERT); GANGLIOSIDES; MANNOSE-6-PHOSPHATE (M6P);

EID: 34547819689     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00463-07     Document Type: Article
Times cited : (49)

References (48)
  • 1
    • 0033529902 scopus 로고    scopus 로고
    • Systemic correction of the muscle disorder glycogen storage disease type II after hepatic targeting of a modified adenovirus vector encoding human acid-α-glucosidase
    • Amalfitano, A., A. J. McVie-Wylie, H. Hu, T. L. Dawson, N. Rabens, P. Plotz, and Y. T. Chen. 1999. Systemic correction of the muscle disorder glycogen storage disease type II after hepatic targeting of a modified adenovirus vector encoding human acid-α-glucosidase. Proc. Natl. Acad. Sci. USA 96:8861-8866.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8861-8866
    • Amalfitano, A.1    McVie-Wylie, A.J.2    Hu, H.3    Dawson, T.L.4    Rabens, N.5    Plotz, P.6    Chen, Y.T.7
  • 2
    • 3242681806 scopus 로고    scopus 로고
    • Improved outcome of N-butyldeoxygalactonojirimycin-mediated substrate reduction therapy in a mouse model of Sandhoff disease
    • Andersson, U., D. Smith, M. Jeyakumar, T. D. Butters, M. C. Bona, R. A. Dwek, and F. M. Platt. 2004. Improved outcome of N-butyldeoxygalactonojirimycin-mediated substrate reduction therapy in a mouse model of Sandhoff disease. Neurobiol. Dis. 16:506-515.
    • (2004) Neurobiol. Dis , vol.16 , pp. 506-515
    • Andersson, U.1    Smith, D.2    Jeyakumar, M.3    Butters, T.D.4    Bona, M.C.5    Dwek, R.A.6    Platt, F.M.7
  • 3
    • 0033936361 scopus 로고    scopus 로고
    • In vivo inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1-deoxygalactonojirimycin and its derivatives
    • Asano, N., S. Ishii, H. Kizu, K. Ikeda, K. Yasuda, A. Kato, O. R. Maritn, and J. Q. Fan. 2000. In vivo inhibition and intracellular enhancement of lysosomal α-galactosidase A activity in Fabry lymphoblasts by 1-deoxygalactonojirimycin and its derivatives. Eur. J. Biochem. 267:4179-4186.
    • (2000) Eur. J. Biochem , vol.267 , pp. 4179-4186
    • Asano, N.1    Ishii, S.2    Kizu, H.3    Ikeda, K.4    Yasuda, K.5    Kato, A.6    Maritn, O.R.7    Fan, J.Q.8
  • 5
    • 0034512968 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis: Application to lysosomal storage disorders
    • Butters, T. D., R. A. Dwek, and F. M. Platt. 2000. Inhibition of glycosphingolipid biosynthesis: application to lysosomal storage disorders. Chem. Rev. 100:4683-4696.
    • (2000) Chem. Rev , vol.100 , pp. 4683-4696
    • Butters, T.D.1    Dwek, R.A.2    Platt, F.M.3
  • 6
    • 0033773239 scopus 로고    scopus 로고
    • Purification and characterization of human α-galactosidase A expressed in insect cells using a baculovirus vector
    • Chen, Y., M. Jin, L. Goodrich, G. Smith, G. Coppola, and D. H. Calhoun. 2000. Purification and characterization of human α-galactosidase A expressed in insect cells using a baculovirus vector. Protein Expr. Purif. 20:228-236.
    • (2000) Protein Expr. Purif , vol.20 , pp. 228-236
    • Chen, Y.1    Jin, M.2    Goodrich, L.3    Smith, G.4    Coppola, G.5    Calhoun, D.H.6
  • 7
    • 0033673087 scopus 로고    scopus 로고
    • Expression and characterization of glycosylated and catalytically active recombinant human α-galactosidase A produced in Pichia pastoris
    • Chen, Y., M. Jin, T. Egborge, G. Coppola, J. Andre, and D. H. Calhoun. 2000. Expression and characterization of glycosylated and catalytically active recombinant human α-galactosidase A produced in Pichia pastoris. Protein Expr. Purif. 20:472-484.
    • (2000) Protein Expr. Purif , vol.20 , pp. 472-484
    • Chen, Y.1    Jin, M.2    Egborge, T.3    Coppola, G.4    Andre, J.5    Calhoun, D.H.6
  • 10
    • 0037192762 scopus 로고    scopus 로고
    • Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor
    • Hancock, M. K., D. J. Haskins, G. Sun, and N. M. Dahms. 2002. Identification of residues essential for carbohydrate recognition by the insulin-like growth factor II/mannose 6-phosphate receptor. J. Biol. Chem. 277:11255-11264.
    • (2002) J. Biol. Chem , vol.277 , pp. 11255-11264
    • Hancock, M.K.1    Haskins, D.J.2    Sun, G.3    Dahms, N.M.4
  • 11
    • 0037033019 scopus 로고    scopus 로고
    • Localization of the carbohydrate recognition sites of the insulin-like growth factor II/mannose 6-phosphate receptor to domains 3 and 9 of the extracytoplasmic region
    • Hancock, M. K., R. D. Yammani, and N. M. Dahms. 2002. Localization of the carbohydrate recognition sites of the insulin-like growth factor II/mannose 6-phosphate receptor to domains 3 and 9 of the extracytoplasmic region. J. Biol. Chem. 277:47205-47212.
    • (2002) J. Biol. Chem , vol.277 , pp. 47205-47212
    • Hancock, M.K.1    Yammani, R.D.2    Dahms, N.M.3
  • 15
    • 0029975138 scopus 로고    scopus 로고
    • Direct determination of the substrate specificity of the α-active site in heterodimeric β-hexosaminidase A
    • Hou, Y., R. Tse, and D. J. Mahuran. 1996. Direct determination of the substrate specificity of the α-active site in heterodimeric β-hexosaminidase A. Biochemistry 35:3963-3969.
    • (1996) Biochemistry , vol.35 , pp. 3963-3969
    • Hou, Y.1    Tse, R.2    Mahuran, D.J.3
  • 16
    • 0031719830 scopus 로고    scopus 로고
    • Increased expression of β-hexosaminidase α chain in cultured skin fibroblasts from patients with carbohydrate-deficient glycoprotein syndrome type I
    • Ichisaka, S., K. Ohno, I. Yuasa, E. Nanba, H. Sakuraba, and Y. Suzuki. 1998. Increased expression of β-hexosaminidase α chain in cultured skin fibroblasts from patients with carbohydrate-deficient glycoprotein syndrome type I. Brain Dev. 20:302-306.
    • (1998) Brain Dev , vol.20 , pp. 302-306
    • Ichisaka, S.1    Ohno, K.2    Yuasa, I.3    Nanba, E.4    Sakuraba, H.5    Suzuki, Y.6
  • 18
    • 18444368694 scopus 로고    scopus 로고
    • Enzyme replacement therapy in classical infantile Pompe disease: Results of a ten-month follow-up study
    • Klinge, L., V. Straub, U. Neudorf, and T. Voit. 2005. Enzyme replacement therapy in classical infantile Pompe disease: results of a ten-month follow-up study. Neuropediatrics 36:6-11.
    • (2005) Neuropediatrics , vol.36 , pp. 6-11
    • Klinge, L.1    Straub, V.2    Neudorf, U.3    Voit, T.4
  • 19
    • 33750025988 scopus 로고    scopus 로고
    • Production of Man5GlcNAc2-type sugar chain by the methylotrophic yeast Ogataea minuta
    • Kuroda, K., K. Kobayashi, H. Tsumura, T. Komeda, Y. Chiba, and Y. Jigami. 2006. Production of Man5GlcNAc2-type sugar chain by the methylotrophic yeast Ogataea minuta. FEMS Yeast Res. 6:1052-1062.
    • (2006) FEMS Yeast Res , vol.6 , pp. 1052-1062
    • Kuroda, K.1    Kobayashi, K.2    Tsumura, H.3    Komeda, T.4    Chiba, Y.5    Jigami, Y.6
  • 20
    • 13844250361 scopus 로고    scopus 로고
    • β-Hexosaminidase lentiviral vectors: Transfer into the CNS via systemic administration
    • Kyrkanides, S., J. H. Miller, M. Brouxhon, J. A. Olschowka, and H. J. Federoff. 2005. β-Hexosaminidase lentiviral vectors: transfer into the CNS via systemic administration. Mol. Brain Res. 133:286-298.
    • (2005) Mol. Brain Res , vol.133 , pp. 286-298
    • Kyrkanides, S.1    Miller, J.H.2    Brouxhon, M.3    Olschowka, J.A.4    Federoff, H.J.5
  • 21
    • 0024788009 scopus 로고
    • A frameshift mutation in a patient with Tay-Sachs disease causes premature termination and defective intracellular transport of the α-subunit of β-hexosaminidase
    • Lau, M. M. H., and E. F. Neufeld. 1989. A frameshift mutation in a patient with Tay-Sachs disease causes premature termination and defective intracellular transport of the α-subunit of β-hexosaminidase. J. Biol. Chem. 264:21376-21380.
    • (1989) J. Biol. Chem , vol.264 , pp. 21376-21380
    • Lau, M.M.H.1    Neufeld, E.F.2
  • 22
    • 33744798282 scopus 로고    scopus 로고
    • Crystallographic structure of human β-hexosaminidase A: Interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis
    • Lemieux, M. J., B. L. Mark, M. M. Cherney, S. G. Withers, D. J. Mahuran, and M. N. G. James. 2006. Crystallographic structure of human β-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis. J. Mol. Biol. 359:913-929.
    • (2006) J. Mol. Biol , vol.359 , pp. 913-929
    • Lemieux, M.J.1    Mark, B.L.2    Cherney, M.M.3    Withers, S.G.4    Mahuran, D.J.5    James, M.N.G.6
  • 23
    • 0021352678 scopus 로고
    • Effect of modification of sialic acid on enzymatic hydrolysis of ganglioside GM1 and GM2
    • Li, S. C., S. Serizawa, and Y. T. Li. 1984. Effect of modification of sialic acid on enzymatic hydrolysis of ganglioside GM1 and GM2. J. Biol. Chem. 259:5409-5410.
    • (1984) J. Biol. Chem , vol.259 , pp. 5409-5410
    • Li, S.C.1    Serizawa, S.2    Li, Y.T.3
  • 24
    • 0023929842 scopus 로고
    • Proteolytic processing of the α-chain of the lysosomal enzyme, β-hexosaminidase, in normal human fibroblasts
    • Little, L. E., M. M. H. Lau, D. V. K. Quon, A. V. Fowler, and E. F. Neufeld. 1988. Proteolytic processing of the α-chain of the lysosomal enzyme, β-hexosaminidase, in normal human fibroblasts. J. Biol. Chem. 263:4288-4292.
    • (1988) J. Biol. Chem , vol.263 , pp. 4288-4292
    • Little, L.E.1    Lau, M.M.H.2    Quon, D.V.K.3    Fowler, A.V.4    Neufeld, E.F.5
  • 25
    • 0037414455 scopus 로고    scopus 로고
    • The X-ray crystal structure of human β-hexosaminidase B provides new insights into Sandhoff disease
    • Maier, T., N. Strater, C. G. Schuette, R. Klingenstein, K. Sandhoff, and W. Saenger. 2003. The X-ray crystal structure of human β-hexosaminidase B provides new insights into Sandhoff disease. J. Mol. Biol. 328:669-681.
    • (2003) J. Mol. Biol , vol.328 , pp. 669-681
    • Maier, T.1    Strater, N.2    Schuette, C.G.3    Klingenstein, R.4    Sandhoff, K.5    Saenger, W.6
  • 26
    • 0344837327 scopus 로고    scopus 로고
    • Crystal structure of human β-hexosaminidase B: Understanding the molecular basis of Sandhoff and Tay-Sachs disease
    • Mark, B. L., D. J. Mahuran, M. M. Cherney, D. Zhao, S. Knapp, and M. N. G. James. 2003. Crystal structure of human β-hexosaminidase B: understanding the molecular basis of Sandhoff and Tay-Sachs disease. J. Mol. Biol. 327:1093-1109.
    • (2003) J. Mol. Biol , vol.327 , pp. 1093-1109
    • Mark, B.L.1    Mahuran, D.J.2    Cherney, M.M.3    Zhao, D.4    Knapp, S.5    James, M.N.G.6
  • 28
    • 0036984005 scopus 로고    scopus 로고
    • Enzyme replacement therapy in mucopolysaccharidosis type II (Hunter syndrome): A preliminary report
    • Muenzer, J., J. C. Lamsa, A. Garcia, J. Dacosta, J. Garcia, and D. A. Treco. 2002. Enzyme replacement therapy in mucopolysaccharidosis type II (Hunter syndrome): a preliminary report. Acta Paediatr. Suppl. 91:98-99.
    • (2002) Acta Paediatr. Suppl , vol.91 , pp. 98-99
    • Muenzer, J.1    Lamsa, J.C.2    Garcia, A.3    Dacosta, J.4    Garcia, J.5    Treco, D.A.6
  • 30
    • 0030475074 scopus 로고    scopus 로고
    • Cloning and analysis of the MNN4 gene required for phosphorylation of N-linked oligosaccharides in Saccharomyces cerevisiae
    • Odani, T., Y. Shimma, A. Tanaka, and Y. Jigami. 1996. Cloning and analysis of the MNN4 gene required for phosphorylation of N-linked oligosaccharides in Saccharomyces cerevisiae. Glycobiology 6:805-810.
    • (1996) Glycobiology , vol.6 , pp. 805-810
    • Odani, T.1    Shimma, Y.2    Tanaka, A.3    Jigami, Y.4
  • 31
    • 0031590758 scopus 로고    scopus 로고
    • Mannosylphosphate transfer to cell wall mannan is regulated by the transcriptional level of the MNN4 gene in Saccharomyces cerevisiae
    • Odani, T., Y. Shimma, X. H. Wang, and Y. Jigami. 1997. Mannosylphosphate transfer to cell wall mannan is regulated by the transcriptional level of the MNN4 gene in Saccharomyces cerevisiae. FEBS Lett. 420:186-190.
    • (1997) FEBS Lett , vol.420 , pp. 186-190
    • Odani, T.1    Shimma, Y.2    Wang, X.H.3    Jigami, Y.4
  • 32
    • 0023008165 scopus 로고
    • Molecular heterogeneity in the infantile and juvenile forms of Sandhoff disease (O-variant GM2 gangliosidosis)
    • O'Dowd, B. F., M. H. Klavins, H. F. Willard, R. Grabel, J. A. Lowden, and D. J. Mahuran. 1986. Molecular heterogeneity in the infantile and juvenile forms of Sandhoff disease (O-variant GM2 gangliosidosis). J. Biol. Chem. 261:12680-12685.
    • (1986) J. Biol. Chem , vol.261 , pp. 12680-12685
    • O'Dowd, B.F.1    Klavins, M.H.2    Willard, H.F.3    Grabel, R.4    Lowden, J.A.5    Mahuran, D.J.6
  • 33
    • 26944444730 scopus 로고    scopus 로고
    • Establishment of immortalized Schwann cells from Sandhoff mice and corrective effect of recombinant human β-hexosaminidase A on the accumulated GM2 ganglioside
    • Ohsawa, M., M. Kotani, Y. Tajima, D. Tsuji, Y. Ishibashi, A. Kuraki, K. Itoh, K. Watabe, K. Sango, S. Yamanaka, and H. Sakuraba. 2005. Establishment of immortalized Schwann cells from Sandhoff mice and corrective effect of recombinant human β-hexosaminidase A on the accumulated GM2 ganglioside. J. Hum. Genet. 50:460-467.
    • (2005) J. Hum. Genet , vol.50 , pp. 460-467
    • Ohsawa, M.1    Kotani, M.2    Tajima, Y.3    Tsuji, D.4    Ishibashi, Y.5    Kuraki, A.6    Itoh, K.7    Watabe, K.8    Sango, K.9    Yamanaka, S.10    Sakuraba, H.11
  • 34
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate
    • Potier, M., L. Mameil, M. Belisle, L. Dallaine, and S. B. Melancon. 1979. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate. Anal. Biochem. 94:287-296.
    • (1979) Anal. Biochem , vol.94 , pp. 287-296
    • Potier, M.1    Mameil, L.2    Belisle, M.3    Dallaine, L.4    Melancon, S.B.5
  • 35
    • 0024550289 scopus 로고
    • Proteolytic processing of the β-subunit of the lysosomal enzyme, β-hexosaminidase, in normal human fibroblasts
    • Quon, D. V. K., R. L. Praia, A. V. Fowler, J. Bleibaum, and E. F. Neufeld. 1989. Proteolytic processing of the β-subunit of the lysosomal enzyme, β-hexosaminidase, in normal human fibroblasts. J. Biol. Chem. 264:3380-3384.
    • (1989) J. Biol. Chem , vol.264 , pp. 3380-3384
    • Quon, D.V.K.1    Praia, R.L.2    Fowler, A.V.3    Bleibaum, J.4    Neufeld, E.F.5
  • 36
    • 4644360229 scopus 로고    scopus 로고
    • Identification of a low affinity mannose 6-phosphate-binding site in domain 5 of the cation-independent mannose 6-phosphate receptor
    • Reddy, S. T., W. Chai, R. A. Childs, J. D. Page, T. Feizi, and N. M. Dahms. 2004. Identification of a low affinity mannose 6-phosphate-binding site in domain 5 of the cation-independent mannose 6-phosphate receptor. J. Biol. Chem. 279:38658-38667.
    • (2004) J. Biol. Chem , vol.279 , pp. 38658-38667
    • Reddy, S.T.1    Chai, W.2    Childs, R.A.3    Page, J.D.4    Feizi, T.5    Dahms, N.M.6
  • 39
    • 0032976576 scopus 로고    scopus 로고
    • Systemic and central nervous system correction of lysosomal storage in mucopolysaccharidosis type VII mice
    • Stein, C. S., A. Ghodsi, T. Derksen, and B. L. Davidson. 1999. Systemic and central nervous system correction of lysosomal storage in mucopolysaccharidosis type VII mice. J. Virol. 73:3424-3429.
    • (1999) J. Virol , vol.73 , pp. 3424-3429
    • Stein, C.S.1    Ghodsi, A.2    Derksen, T.3    Davidson, B.L.4
  • 40
    • 33746224098 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in N-linked glycans by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Takashiba, M., Y. Chiba, and Y. Jigami. 2006. Identification of phosphorylation sites in N-linked glycans by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Chem. 78:5208-5213.
    • (2006) Anal. Chem , vol.78 , pp. 5208-5213
    • Takashiba, M.1    Chiba, Y.2    Jigami, Y.3
  • 41
    • 0001250942 scopus 로고
    • β-N- Acetylglucosaminidase from hen oviduct
    • Tarentino, A. L., and F. Maley. 1972. β-N- Acetylglucosaminidase from hen oviduct. Methods Enzymol. 28:772-776.
    • (1972) Methods Enzymol , vol.28 , pp. 772-776
    • Tarentino, A.L.1    Maley, F.2
  • 42
    • 1842741341 scopus 로고    scopus 로고
    • Pharmacological enhancement of β-hexosaminidase activity in fibroblasts from adult Tay-Sachs and Sandhoff patients
    • Trapak, M. B., S. P. Reid, M. Guiral, S. G. Withers, and D. Mahuran. 2004. Pharmacological enhancement of β-hexosaminidase activity in fibroblasts from adult Tay-Sachs and Sandhoff patients. J. Biol. Chem. 279:13478-13487.
    • (2004) J. Biol. Chem , vol.279 , pp. 13478-13487
    • Trapak, M.B.1    Reid, S.P.2    Guiral, M.3    Withers, S.G.4    Mahuran, D.5
  • 43
    • 0023784539 scopus 로고
    • Intracellular transport of acid α-glucosidase in human fibroblasts: Evidence for involvement of phosphomannosyl receptor-independent system
    • Tsuji, A., K. Omura, and Y. Suzuki. 1988. Intracellular transport of acid α-glucosidase in human fibroblasts: evidence for involvement of phosphomannosyl receptor-independent system. J. Biochem. 104:276-278.
    • (1988) J. Biochem , vol.104 , pp. 276-278
    • Tsuji, A.1    Omura, K.2    Suzuki, Y.3
  • 44
    • 24944553351 scopus 로고    scopus 로고
    • Metabolic correction in microglia derived from Sandhoff disease model mice
    • Tsuji, D., A. Kuroki, Y. Ishibashi, T. Itakura, and K. Itoh. 2005. Metabolic correction in microglia derived from Sandhoff disease model mice. J. Neurochem. 94:1631-1638.
    • (2005) J. Neurochem , vol.94 , pp. 1631-1638
    • Tsuji, D.1    Kuroki, A.2    Ishibashi, Y.3    Itakura, T.4    Itoh, K.5
  • 45
    • 2942570942 scopus 로고    scopus 로고
    • Van den Hout, J. M. P., J. H. J. Kamphoven, L. P. F. Winkel, W. F. M. Arts, J. B. C. de Klerk, M. C. B. Loonen, A. G. Vulto, A. Cramme-Dijkhuis, N. Weisglas-Kuperus, W. Hop, H. van Hirtum, O. P. van Diggelen, M. Boer, M. A. Kroos, P. A. van Doom, E. van der Voort, B. Sibbles, E. J. J. M. van Corven, J. P. J. Brakenhoff, J. van Hove, J. A. M. Smeitink, G. de Jong, A. J. J. Reuser, and A. T. van der Ploeg. 2004. Long-term intravenous treatment of Pompe disease with recombinant human α-glucosidase from milk. Pediatrics 113:e448-e457.
    • Van den Hout, J. M. P., J. H. J. Kamphoven, L. P. F. Winkel, W. F. M. Arts, J. B. C. de Klerk, M. C. B. Loonen, A. G. Vulto, A. Cramme-Dijkhuis, N. Weisglas-Kuperus, W. Hop, H. van Hirtum, O. P. van Diggelen, M. Boer, M. A. Kroos, P. A. van Doom, E. van der Voort, B. Sibbles, E. J. J. M. van Corven, J. P. J. Brakenhoff, J. van Hove, J. A. M. Smeitink, G. de Jong, A. J. J. Reuser, and A. T. van der Ploeg. 2004. Long-term intravenous treatment of Pompe disease with recombinant human α-glucosidase from milk. Pediatrics 113:e448-e457.
  • 47
    • 4444244233 scopus 로고    scopus 로고
    • Efficient and rapid purification of recombinant human α-galacotosidase A by affinity column chromatography
    • Yasuda, K., H. H. Chang, H. L. Wu, S. Ishii, and J. Q. Fan. 2004. Efficient and rapid purification of recombinant human α-galacotosidase A by affinity column chromatography. Protein Expr. Purif. 37:499-506.
    • (2004) Protein Expr. Purif , vol.37 , pp. 499-506
    • Yasuda, K.1    Chang, H.H.2    Wu, H.L.3    Ishii, S.4    Fan, J.Q.5


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