The clinical effectiveness and cost-effectiveness of enzyme replacement therapy for Gaucher's disease: a systematic review

West Midlands Health Technology Assessment Collaboration (WMHTAC), University of Birmingham, UK.
Health technology assessment (Winchester, England) (Impact Factor: 5.12). 08/2006; 10(24). DOI: 10.3310/hta10240
Source: OAI

ABSTRACT see also

Download full-text


Available from: Christopher Mccabe, Oct 21, 2014
1 Follower
  • Source
    Novel Aspects on Epilepsy, 10/2011; , ISBN: 978-953-307-678-2
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Lysosomal storage diseases are a group of disorders caused by defects in enzymes responsible for degradation of particular compounds in lysosomes. In most cases, these diseases are fatal, and until recently no treatment was available. Introduction of enzyme replacement therapy was a breakthrough in the treatment of some of the diseases. However, while this therapy is effective in reduction of many somatic symptoms, its efficacy in the treatment of the central nervous system is negligible, if any, mainly because of problems with crossing the blood-brain-barrier by intravenously administered enzyme molecules. On the other hand, there are many lysosomal storage diseases in which the central nervous system is affected. Results of very recent studies indicate that in at least some cases, another type of therapy, called substrate deprivation therapy (or substrate reduction therapy) may be effective in the treatment of neuronopathic forms of lysosomal storage diseases. This therapy, based on inhibition of synthesis of the compounds that cannot be degraded in cells of the patients, has been shown to be effective in several animal models of various diseases, and recent reports demonstrate its efficacy in the treatment of patients suffering from Niemann-Pick C disease and Sanfilippo disease.
    Journal of applied genetics 02/2007; 48(4):383-8. DOI:10.1007/BF03195237 · 1.90 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: The mutations in human glucosylceramidase lead to Gaucher disease, which is the most prevalent lysosomal storage disease. So far 153 point mutations have been recorded in human glucosylceramidase, resulting in a wide variability in clinical presentations. In this study, we use the amino-acid distribution probability to quantify each mutation, and use the cross-impact analysis with Bayes’ law to build a quantitative relationship between mutated primary structure of human glucosylceramidase and status of Gaucher disease. The results demonstrate that we can build a quantitative relationship between changed structure and changed function of protein, which is useful for understanding the genotype–phenotype relationship of disease.
    International Journal of Peptide Research and Therapeutics 09/2008; 14(3):263-271. DOI:10.1007/s10989-008-9142-3 · 0.83 Impact Factor