Literature DB >> 17689998

Influence of antibody formation on reduction of globotriaosylceramide (GL-3) in urine from Fabry patients during agalsidase beta therapy.

Toya Ohashi1, Mio Sakuma, Teruo Kitagawa, Ken Suzuki, Nobuyuki Ishige, Yoshikatsu Eto.   

Abstract

Two recombinant human agalsidase preparations are available for treatment of Fabry disease. We assayed urinary GL-3 (uGL-3) concentration in seronegative and seropositive patients receiving agalsidase beta (1mg/kg). Antibody formation and residual enzyme activity were strongly correlated. Normalization of uGL-3 was achieved more efficiently in seronegatives. But different from previous reports, reduction of uGL-3 level was observed in some seropositive patients.

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Year:  2007        PMID： 17689998     DOI： 10.1016/j.ymgme.2007.06.013

Source DB:  PubMed          Journal:  Mol Genet Metab        ISSN： 1096-7192            Impact factor:   4.797


  13 in total

Review 1.  Fabry disease, enzyme replacement therapy and the significance of antibody responses.

Authors:  Patrick B Deegan
Journal:  J Inherit Metab Dis       Date:  2011-10-25       Impact factor: 4.982

2.  Enzyme therapy in Fabry disease: severe adverse events associated with anti-agalsidase cross-reactive IgG antibodies.

Authors:  Chloe Tesmoingt; Olivier Lidove; Axele Reberga; Marguerite Thetis; Chloe Ackaert; Pascale Nicaise; Philippe Arnaud; Thomas Papo
Journal:  Br J Clin Pharmacol       Date:  2009-11       Impact factor: 4.335

3.  Effect of reduced agalsidase Beta dosage in fabry patients: the Australian experience.

Authors:  Joanna Ghali; Kathy Nicholls; Charles Denaro; David Sillence; Ian Chapman; Jack Goldblatt; Mark Thomas; Janice Fletcher
Journal:  JIMD Rep       Date:  2011-09-15

4.  Recommendations on reintroduction of agalsidase Beta for patients with fabry disease in europe, following a period of shortage.

Authors:  Gabor E Linthorst; Alessandro P Burlina; Franco Cecchi; Timothy M Cox; Janice M Fletcher; Ulla Feldt-Rasmussen; Roberto Giugliani; Carla E M Hollak; Gunnar Houge; Derralynn Hughes; Iikka Kantola; Robin Lachmann; Monica Lopez; Alberto Ortiz; Rossella Parini; Alberto Rivera; Arndt Rolfs; Uma Ramaswami; Einar Svarstad; Camilla Tondel; Anna Tylki-Szymanska; Bojan Vujkovac; Steven Waldek; Michael West; F Weidemann; Atul Mehta
Journal:  JIMD Rep       Date:  2012-07-14

5.  Administration of anti-CD3 antibodies modulates the immune response to an infusion of α-glucosidase in mice.

Authors:  Toya Ohashi; Sayoko Iizuka; Yohta Shimada; Takashi Higuchi; Yoshikatsu Eto; Hiroyuki Ida; Hiroshi Kobayashi
Journal:  Mol Ther       Date:  2012-08-07       Impact factor: 11.454

6.  Elevated globotriaosylsphingosine is a hallmark of Fabry disease.

Authors:  Johannes M Aerts; Johanna E Groener; Sijmen Kuiper; Wilma E Donker-Koopman; Anneke Strijland; Roelof Ottenhoff; Cindy van Roomen; Mina Mirzaian; Frits A Wijburg; Gabor E Linthorst; Anouk C Vedder; Saskia M Rombach; Josanne Cox-Brinkman; Pentti Somerharju; Rolf G Boot; Carla E Hollak; Roscoe O Brady; Ben J Poorthuis
Journal:  Proc Natl Acad Sci U S A       Date:  2008-02-19       Impact factor: 11.205

7.  Non-invasive high-risk screening for Fabry disease hemizygotes and heterozygotes.

Authors:  Teruo Kitagawa; Ken Suzuki; Nobuyuki Ishige; Toya Ohashi; Masahisa Kobayashi; Yoshikatsu Eto; Akemi Tanaka; Hideo Odaka; Misao Owada
Journal:  Pediatr Nephrol       Date:  2008-06-06       Impact factor: 3.714

Review 8.  Enzyme replacement therapy for Fabry disease: a systematic review of available evidence.

Authors:  Roland M Schaefer; Anna Tylki-Szymańska; Max J Hilz
Journal:  Drugs       Date:  2009-11-12       Impact factor: 9.546

9.  Use of a modified alpha-N-acetylgalactosaminidase in the development of enzyme replacement therapy for Fabry disease.

Authors:  Youichi Tajima; Ikuo Kawashima; Takahiro Tsukimura; Kanako Sugawara; Mayuko Kuroda; Toshihiro Suzuki; Tadayasu Togawa; Yasunori Chiba; Yoshifumi Jigami; Kazuki Ohno; Tomoko Fukushige; Takuro Kanekura; Kohji Itoh; Toya Ohashi; Hitoshi Sakuraba
Journal:  Am J Hum Genet       Date:  2009-10-22       Impact factor: 11.025

10.  Carboxyl-terminal truncations alter the activity of the human α-galactosidase A.

Authors:  Mariam Meghdari; Nicholas Gao; Abass Abdullahi; Erin Stokes; David H Calhoun
Journal:  PLoS One       Date:  2015-02-26       Impact factor: 3.240
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