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Volumn 85, Issue 5, 2009, Pages 569-580

Use of a Modified α-N-Acetylgalactosaminidase in the Development of Enzyme Replacement Therapy for Fabry Disease

Author keywords

[No Author keywords available]

Indexed keywords

4 METHYLUMBERLLIFERYL ALPHA DEXTRO GALACTOPYRANOSIDE; AGALSIDASE ALFA; AGALSIDASE BETA; ALPHA GALACTOSIDASE; ALPHA N ACETYLGALACTOSAMINIDASE; GLOBOTRIAOSYLCERAMIDE; MANNOSE 6 PHOSPHATE; MODIFIED ALPHA N ACETYLGALACTOSAMINIDASE; PYRANOSIDE; RECOMBINANT ENZYME; RETROVIRUS VECTOR; SOMATOMEDIN B RECEPTOR; UNCLASSIFIED DRUG;

EID: 71849085606     PISSN: 00029297     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ajhg.2009.09.016     Document Type: Article
Times cited : (48)

References (40)
  • 1
    • 0000889058 scopus 로고    scopus 로고
    • alpha-Galactosidase A deficiency: Fabry disease
    • Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds), McGraw-Hill, New York, USA
    • Desnick R.J., Ioannou Y.A., and Eng C.M. alpha-Galactosidase A deficiency: Fabry disease. In: Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds). The Metabolic and Molecular Bases of Inherited Disease. Eighth Edition (2001), McGraw-Hill, New York, USA 3733-3774
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. Eighth Edition , pp. 3733-3774
    • Desnick, R.J.1    Ioannou, Y.A.2    Eng, C.M.3
  • 6
    • 0001261457 scopus 로고    scopus 로고
    • I-cell disease and pseudo-Hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization
    • Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds), McGraw-Hill, New York
    • Kornfeld S., and Sly W.S. I-cell disease and pseudo-Hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization. In: Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds). The Metabolic and Molecular Bases of Inherited Disease. Eighth Edition (2001), McGraw-Hill, New York 3469-3482
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. Eighth Edition , pp. 3469-3482
    • Kornfeld, S.1    Sly, W.S.2
  • 8
    • 34848819423 scopus 로고    scopus 로고
    • Influence of antibody formation on reduction of globotriaosylceramide (GL-3) in urine from Fabry patients during agalsidase beta therapy
    • Ohashi T., Sakuma M., Kitagawa T., Suzuki K., Ishige N., and Eto Y. Influence of antibody formation on reduction of globotriaosylceramide (GL-3) in urine from Fabry patients during agalsidase beta therapy. Mol. Genet. Metab. 92 (2007) 271-273
    • (2007) Mol. Genet. Metab. , vol.92 , pp. 271-273
    • Ohashi, T.1    Sakuma, M.2    Kitagawa, T.3    Suzuki, K.4    Ishige, N.5    Eto, Y.6
  • 9
    • 44649172457 scopus 로고    scopus 로고
    • Reduced alpha-Gal A enzyme activity in Fabry fibroblast cells and Fabry mice tissues induced by serum from antibody positive patients with Fabry disease
    • Ohashi T., Iizuka S., Ida H., and Eto Y. Reduced alpha-Gal A enzyme activity in Fabry fibroblast cells and Fabry mice tissues induced by serum from antibody positive patients with Fabry disease. Mol. Genet. Metab. 94 (2008) 313-318
    • (2008) Mol. Genet. Metab. , vol.94 , pp. 313-318
    • Ohashi, T.1    Iizuka, S.2    Ida, H.3    Eto, Y.4
  • 11
    • 0006825324 scopus 로고
    • Fabry disease: α-galactosidase A deficiency
    • Glew R.H., and Peters S.P. (Eds), Alan R. Liss, New York
    • Dean K.J., and Sweeley C.C. Fabry disease: α-galactosidase A deficiency. In: Glew R.H., and Peters S.P. (Eds). Practical Enzymology of the Sphingolipidoses (1977), Alan R. Liss, New York 173-216
    • (1977) Practical Enzymology of the Sphingolipidoses , pp. 173-216
    • Dean, K.J.1    Sweeley, C.C.2
  • 13
    • 0036124422 scopus 로고    scopus 로고
    • The 1.9 Å structure of α-N-acetylgalactosaminidase: Molecular basis of glycosidase deficiency diseases
    • Garman S.C., Hannick L., Zhu A., and Garboczi D.N. The 1.9 Å structure of α-N-acetylgalactosaminidase: Molecular basis of glycosidase deficiency diseases. Structure 10 (2002) 425-434
    • (2002) Structure , vol.10 , pp. 425-434
    • Garman, S.C.1    Hannick, L.2    Zhu, A.3    Garboczi, D.N.4
  • 14
    • 1442299241 scopus 로고    scopus 로고
    • The molecular defect leading to Fabry disease: Structure of human alpha-galactosidase
    • Garman S.C., and Garboczi D.N. The molecular defect leading to Fabry disease: Structure of human alpha-galactosidase. J. Mol. Biol. 337 (2004) 319-335
    • (2004) J. Mol. Biol. , vol.337 , pp. 319-335
    • Garman, S.C.1    Garboczi, D.N.2
  • 15
    • 84986432905 scopus 로고
    • Accurate modeling of the intramolecular electrostatic energy of proteins
    • Dudek M.J., and Ponder J.W. Accurate modeling of the intramolecular electrostatic energy of proteins. J. Comput. Chem. 16 (1995) 791-816
    • (1995) J. Comput. Chem. , vol.16 , pp. 791-816
    • Dudek, M.J.1    Ponder, J.W.2
  • 16
    • 84962376142 scopus 로고    scopus 로고
    • Calculation of the reaction field due to off-center point multipoles
    • Kong M.J., and Ponder J.W. Calculation of the reaction field due to off-center point multipoles. J. Chem. Phys. 107 (1997) 481-492
    • (1997) J. Chem. Phys. , vol.107 , pp. 481-492
    • Kong, M.J.1    Ponder, J.W.2
  • 17
    • 0038424321 scopus 로고    scopus 로고
    • Analysis and application of potential energy smoothing for global optimization
    • Pappu R.V., Hart R.K., and Ponder J.W. Analysis and application of potential energy smoothing for global optimization. J. Phys. Chem. B 102 (1998) 9725-9742
    • (1998) J. Phys. Chem. B , vol.102 , pp. 9725-9742
    • Pappu, R.V.1    Hart, R.K.2    Ponder, J.W.3
  • 18
    • 0037899660 scopus 로고    scopus 로고
    • Polarizable atomic multipole water model for molecular mechanics simulation
    • Ren P., and Ponder J.W. Polarizable atomic multipole water model for molecular mechanics simulation. J. Phys. Chem. B 107 (2003) 5933-5947
    • (2003) J. Phys. Chem. B , vol.107 , pp. 5933-5947
    • Ren, P.1    Ponder, J.W.2
  • 19
    • 0019464277 scopus 로고
    • Differential assay for lysosomal α-galactosidases in human tissues and its application to Fabry's disease
    • Mayes J.S., Scheerer J.B., Sifers R.N., and Donaldson M.L. Differential assay for lysosomal α-galactosidases in human tissues and its application to Fabry's disease. Clin. Chim. Acta 112 (1981) 247-251
    • (1981) Clin. Chim. Acta , vol.112 , pp. 247-251
    • Mayes, J.S.1    Scheerer, J.B.2    Sifers, R.N.3    Donaldson, M.L.4
  • 21
    • 0344823945 scopus 로고    scopus 로고
    • Refractory nature of normal human diploid fibroblasts with respect to oncogene-mediated transformation
    • Akagi T., Sasai K., and Hanafusa H. Refractory nature of normal human diploid fibroblasts with respect to oncogene-mediated transformation. Proc. Natl. Acad. Sci. USA 100 (2003) 13567-13572
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13567-13572
    • Akagi, T.1    Sasai, K.2    Hanafusa, H.3
  • 22
    • 45149083131 scopus 로고    scopus 로고
    • Rapid production of retroviruses for efficient gene delivery to mammalian cells using 293T cell-based systems
    • Coligan J.E. (Ed), John Wiley and Sons, New York
    • Swift S., Lorens J., Achacoso P., and Nolan G.P. Rapid production of retroviruses for efficient gene delivery to mammalian cells using 293T cell-based systems. In: Coligan J.E. (Ed). Current Protocols in Immunology (2001), John Wiley and Sons, New York 10.17.14-10.17.29
    • (2001) Current Protocols in Immunology
    • Swift, S.1    Lorens, J.2    Achacoso, P.3    Nolan, G.P.4
  • 25
    • 61849099371 scopus 로고    scopus 로고
    • Molecular interaction of imino sugars with human alpha-galactosidase: Insight into the mechanism of complex formation and pharmacological chaperone action in Fabry disease
    • Sugawara K., Tajima Y., Kawashima I., Tsukimura T., Saito S., Ohno K., Iwamoto K., Kobayashi T., Itoh K., and Sakuraba H. Molecular interaction of imino sugars with human alpha-galactosidase: Insight into the mechanism of complex formation and pharmacological chaperone action in Fabry disease. Mol. Genet. Metab. 96 (2009) 233-238
    • (2009) Mol. Genet. Metab. , vol.96 , pp. 233-238
    • Sugawara, K.1    Tajima, Y.2    Kawashima, I.3    Tsukimura, T.4    Saito, S.5    Ohno, K.6    Iwamoto, K.7    Kobayashi, T.8    Itoh, K.9    Sakuraba, H.10
  • 26
    • 34648833446 scopus 로고    scopus 로고
    • Enzyme replacement in Fabry disease: Pharmacokinetics and pharmacodynamics of agalsidase alfa in children and adolescents
    • Ries M., Clarke J.T., Whybra C., Mehta A., Loveday K.S., Brady R.O., Beck M., and Schiffmann R. Enzyme replacement in Fabry disease: Pharmacokinetics and pharmacodynamics of agalsidase alfa in children and adolescents. J. Clin. Pharmacol. 47 (2007) 1222-1230
    • (2007) J. Clin. Pharmacol. , vol.47 , pp. 1222-1230
    • Ries, M.1    Clarke, J.T.2    Whybra, C.3    Mehta, A.4    Loveday, K.S.5    Brady, R.O.6    Beck, M.7    Schiffmann, R.8
  • 27
    • 0028216629 scopus 로고
    • Generation of one set of murine monoclonal antibodies specific for globo-series glycolipids: Evidence for differential distribution of the glycolipids in rat small intestine
    • Kotani M., Kawashima I., Ozawa H., Ogura K., Ariga T., and Tai T. Generation of one set of murine monoclonal antibodies specific for globo-series glycolipids: Evidence for differential distribution of the glycolipids in rat small intestine. Arch. Biochem. Biophys. 310 (1994) 89-96
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 89-96
    • Kotani, M.1    Kawashima, I.2    Ozawa, H.3    Ogura, K.4    Ariga, T.5    Tai, T.6
  • 30
    • 0035163539 scopus 로고    scopus 로고
    • Fabry disease: Preclinical studies demonstrate the effectiveness of α-galactosidase A replacement in enzyme-deficient mice
    • Ioannou Y.A., Zeidner K.M., Gordon R.E., and Desnick R.J. Fabry disease: Preclinical studies demonstrate the effectiveness of α-galactosidase A replacement in enzyme-deficient mice. Am. J. Hum. Genet. 68 (2001) 14-25
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 14-25
    • Ioannou, Y.A.1    Zeidner, K.M.2    Gordon, R.E.3    Desnick, R.J.4
  • 32
    • 4644316602 scopus 로고    scopus 로고
    • Enzyme therapy for Fabry disease: Neutralizing antibodies toward agalsidase alpha and beta
    • Linthorst G.E., Hollak C.E., Donker-Koopman W.E., Strijland A., and Aerts J.M. Enzyme therapy for Fabry disease: Neutralizing antibodies toward agalsidase alpha and beta. Kidney Int. 66 (2004) 1589-1595
    • (2004) Kidney Int. , vol.66 , pp. 1589-1595
    • Linthorst, G.E.1    Hollak, C.E.2    Donker-Koopman, W.E.3    Strijland, A.4    Aerts, J.M.5
  • 33
    • 44449108760 scopus 로고    scopus 로고
    • Successful reinstitution of agalsidase beta therapy in Fabry disease patients with previous IgE-antibody or skin-test reactivity to the recombinant enzyme
    • Bodensteiner D., Scott C.R., Sims K.B., Shepherd G.M., Cintron R.D., and Germain D.P. Successful reinstitution of agalsidase beta therapy in Fabry disease patients with previous IgE-antibody or skin-test reactivity to the recombinant enzyme. Genet. Med. 10 (2008) 353-358
    • (2008) Genet. Med. , vol.10 , pp. 353-358
    • Bodensteiner, D.1    Scott, C.R.2    Sims, K.B.3    Shepherd, G.M.4    Cintron, R.D.5    Germain, D.P.6
  • 34
    • 0002568871 scopus 로고    scopus 로고
    • alpha-N-Acetylgalactosaminidase deficiency: Schindler disease
    • Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds), McGraw-Hill, New York
    • Desnick R.J., and Schindler D. alpha-N-Acetylgalactosaminidase deficiency: Schindler disease. In: Scriver C.R., Beaudet A.L., Sly W.S., and Valle D. (Eds). The Metabolic and Molecular Bases of Inherited Disease. Eighth Edition (2001), McGraw-Hill, New York 3483-3505
    • (2001) The Metabolic and Molecular Bases of Inherited Disease. Eighth Edition , pp. 3483-3505
    • Desnick, R.J.1    Schindler, D.2
  • 35
    • 0015524049 scopus 로고
    • Purification and properties of human alpha-galactosidases
    • Beutler E., and Kuhl W. Purification and properties of human alpha-galactosidases. J. Biol. Chem. 247 (1972) 7195-7200
    • (1972) J. Biol. Chem. , vol.247 , pp. 7195-7200
    • Beutler, E.1    Kuhl, W.2
  • 36
    • 0017350660 scopus 로고
    • The identity of alpha-galactosidase B from human liver
    • Schram A.W., Hamers M.N., and Tager J.M. The identity of alpha-galactosidase B from human liver. Biochim. Biophys. Acta 482 (1977) 138-144
    • (1977) Biochim. Biophys. Acta , vol.482 , pp. 138-144
    • Schram, A.W.1    Hamers, M.N.2    Tager, J.M.3
  • 37
    • 0034017142 scopus 로고    scopus 로고
    • Human α-N-acetylgalactosaminidase: Site occupancy and structure of N-linked oligosaccharide
    • Ohta M., Ohnishi T., Ioannou Y.A., Hodgson M.E., Matsuura F., and Desnick R.J. Human α-N-acetylgalactosaminidase: Site occupancy and structure of N-linked oligosaccharide. Glycobiology 10 (2000) 251-261
    • (2000) Glycobiology , vol.10 , pp. 251-261
    • Ohta, M.1    Ohnishi, T.2    Ioannou, Y.A.3    Hodgson, M.E.4    Matsuura, F.5    Desnick, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.