Comparison of the effects of agalsidase alfa and agalsidase beta on cultured human Fabry fibroblasts and Fabry mice

Journal of Human Genetics - Tập 51 Số 3 - Trang 180-188 - 2006
Hitoshi Sakuraba1, Mai Murata-Ohsawa1, Ichiro Kawashima1, Youichi Tajima1, Masaharu Kotani1, Toshio Ohshima2, Yasunori Chiba3, Minako Takashiba3, Yoshifumi Jigami3, Tomoko Fukushige4, Tamotsu Kanzaki4, Kohji Itoh5
1Department of Clinical Genetics, The Tokyo Metropolitan Institute of Medical Science, Tokyo Metropolitan Organization for Medical Research, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan
2Laboratory for Developmental Neurology, Brain Science Institute, RIKEN, Wako, Japan
3Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan
4Department of Dermatology, Kagoshima University Graduate School of Medical and Dental Sciences, Kagoshima, Japan
5Department of Medicinal Biotechnology, Institute for Medicinal Resources, Graduate School of Pharmaceutical Sciences, The University of Tokushima, Tokushima, Japan.

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Desnick RJ, Ioannou YA, Eng CM (2001) α-Galactosidase A deficiency: Fabry disease. In: Scriver CR, Beaudet AL, Sly WS, Valle D (eds) The metabolic and molecular bases of inherited disease, 8th edn. McGraw-Hill, New York, pp 3733–3774

Desnick RJ, Brady RO, Barranger J, Collins AJ, Germain DP, Goldman M, Grabowski G, Packman S, Wilcox WR (2003) Fabry disease, an under-recognized multisystemic disorder: expert recommendations for diagnosis, management, and enzyme replacement therapy. Ann Int Med 138:338–346

Eng CM, Banikazemi M, Gordon RE, Goldman M, Phelps R, Kim L, Gass A, Winston J, Dikman S, Fallon JT, Brodie S, Stacy CB, Mehta D, Parsons R, Norton K, O’Callaghan M, Desnick RJ (2001a) A phase 1/2 clinical trial of enzyme replacement in Fabry disease: pharmacokinetic, substrate clearance, and safety studies. Am J Hum Genet 68:711–722

Eng CM, Guffon N, Wilcox WR, Germain DP, Lee P, Waldek S, Caplan L, Linthorst GE, Desnick RJ (2001b) Safety and efficacy of recombinant human α-galactosidase A replacement therapy in Fabry’s disease. N Engl J Med 345:9–16

Ioannou YA, Zeidner KM, Gordon RE, Desnick RJ (2001) Fabry disease: preclinical studies demonstrate the effectiveness of α-galactosidase A replacement in enzyme-deficient mice. Am J Hum Genet 68:14–25

Ishii S, Kase R, Sakuraba H, Fujita S, Sugimoto M, Tomita K, Semba T, Suzuki Y (1994) Human α-galactosidase gene expression: significance of two peptide regions encoded by exons 1–2 and 6. Biochim Biophys Acta 1204:265–270

Kornfeld S, Sly WS (2001) I-cell disease and pseudo-Hurler polydystrophy: disorders of lysosomal enzyme phosphorylation and localization. In: Scriver CR, Beaudet AL, Sly WS, Valle D (eds) The metabolic and molecular bases of inherited disease, 8th edn. McGraw-Hill, New York, pp 3469–3482

Kotani M, Kawashima I, Ozawa H, Ogura K, Ariga T, Tai T (1994) 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 310:89–96

Lee K, Jin X, Zhang K, Copertino L, Andrews L, Baker-Malcolm J, Geagan L, Qiu H, Seiger K, Barngrover D, McPherson JM, Edmunds T (2003) A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease. Glycobiology 13:305–313

Mayes JS, Scheerer JB, Sifers RN, Donaldson ML (1981) Differential assay for lysosomal α-galactosidase in human tissues and its application to Fabry’s disease. Clin Chim Acta 112:247–251

Mehta A, Ricci R, Widmer U, Dehout F, Garcia de Lorenzo A, Kampmann C, Linhart A, Sunder-Plassmann G, Ries M, Beck M (2004) Fabry disease defined: baseline clinical manifestations of 366 patients in the Fabry Outcome Survey. Eur J Clin Invest 34:236–242

Nakao S, Takenaka T, Maeda M, Kodama C, Tanaka A, Tahara M, Yoshida A, Kuriyama M, Hayashibe H, Sakuraba H, Tanaka H (1995) An atypical variant of Fabry’s disease in men with left ventricular hypertrophy. N Engl J Med 333:288–293

Ohshima T, Murray GJ, Swaim WD, Longenecker G, Quirk JM, Cardarelli CO, Sugimoto Y, Pastan I, Gottesman MM, Brady RO, Kulkarni AB (1997) α-Galactosidase A deficient mice: a model of Fabry disease. Proc Natl Acad Sci USA 94:2540–2544

Ohshima T, Schiffmann R, Murray GJ, Kopp J, Quirk JM, Stahl S, Chan C-C, Zerfas P, Tao-Cheng J-H, Ward JM, Brady RO, Kalkarni AB (1999) Aging accentuates and bone marrow transplantation ameliorates metabolic defects in Fabry disease mice. Proc Natl Acad Sci USA 96:6423–6427

Rosenfeld EL, Belenky DM, Bystrov NK (1986) Interaction of hepatic asialoglycoprotein receptor with asialoorosomucoid and galactolyzed lysosomal α-glucosidase. Biochim Biophys Acta 883:306–312

Schiffmann R, Murray GJ, Treco D, Daniel P, Sellos-Moura M, Myers M, Quirk JM, Zirzow GC, Borowski M, Loveday K, Anderson T, Gillespie F, Cliver KL, Jeffries NO, Doo E, Liang TJ, Kreps C, Gunter K, Frei K, Crutchfield K, Selden RF, Brady RO (2000) Infusion of α-galactosidase A reduces tissue globotriaosylceramide storage in patients with Fabry disease. Proc Natl Acad Sci USA 97:365–370

Takashiba M, Chiba Y, Arai E, Jigami Y (2004) Analysis of mannose-6-phosphate labeled with 8-aminopyrene-1,3,6-trisulfonate by capillary electrophoresis. Anal Biochem 332:196–198

Thurnberg BL, Rennke H, Colvin RB, Dikman S, Gordon RE, Collins AB Desnick RJ, O’Callaghan M (2002) Globotriaosylceramide accumulation in the Fabry kidney is cleared from multiple cell types after enzyme replacement therapy. Kidney Int 62:1933–1946