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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2015.1
- 수록면
- 438 - 444 (7page)
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Lysosomal storage diseases (LSDs) are a group of inherent diseases characterized by massive accumulation of undigested compounds in lysosomes, which is caused by genetic defects resulting in the deficiency of a lysosomal hydrolase. Currently, enzyme replacement therapy has been successfully used for treatment of 7 LSDs with 10 approved therapeutic enzymes whereas new approaches such as pharmacological chaperones and gene therapy still await evaluation in clinical trials. While therapeutic enzymes for Gaucher disease have N-glycans with terminal mannose residues for targeting to macrophages, the others require N-glycans containing mannose-6-phosphates that are recognized by mannose-6-phosphate receptors on the plasma membrane for cellular uptake and targeting to lysosomes. Due to the fact that efficient lysosomal delivery of therapeutic enzymes is essential for the clearance of accumulated compounds, the suitable glycan structure and its high content are key factors for efficient therapeutic efficacy.
Therefore, glycan remodeling strategies to improve lysosomal targeting and tissue distribution have been highlighted. This review describes the glycan structures that are important for lysosomal targeting and provides information on recent glyco- engineering technologies for the development of therapeutic enzymes with improved efficacy.
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참고문헌 (39)
참고문헌 신청
Berger J / 2012 / The uptake of recombinant glucocerebrosidases by blood monocytes from type 1 Gaucher disease patients is variable / Br J Haematol 157:274~277
Van Patten SM / 2007 / Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease / Glycobiology 17:467~478
Koeberl DD / 2011 / Enhanced efficacy of enzyme replacement therapy in Pompe disease through mannose-6-phosphate receptor expression in skeletal muscle / Mol Genet Metab 103:107~112
Chavez CA / 2007 / Domain 5 of the cation-independent mannose 6-phosphate receptor preferentially binds phosphodiesters(mannose 6-phosphate N-acetylglucosamine ester) / Biochemistry 46:12604~12617
Zhu Y / 2004 / Conjugation of mannose 6-phosphate-containing oligosaccharides to acid alpha-glucosidase improves the clearance of glycogen in pompe mice / J Biol Chem 279:50336~50341
Van Patten SM / 2007 / Effect of mannose chain length on targeting of glucocerebrosidase for enzyme replacement therapy of Gaucher disease / Glycobiology 17:467~478
Koeberl DD / 2011 / Enhanced efficacy of enzyme replacement therapy in Pompe disease through mannose-6-phosphate receptor expression in skeletal muscle / Mol Genet Metab 103:107~112
Chavez CA / 2007 / Domain 5 of the cation-independent mannose 6-phosphate receptor preferentially binds phosphodiesters(mannose 6-phosphate N-acetylglucosamine ester) / Biochemistry 46:12604~12617
Zhu Y / 2004 / Conjugation of mannose 6-phosphate-containing oligosaccharides to acid alpha-glucosidase improves the clearance of glycogen in pompe mice / J Biol Chem 279:50336~50341
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