Enzyme Replacement in Nervous Tissue After Allogeneic Bone-Marrow Transplantation for Fucosidosis in Dogs

Taylor, Rabun; Stewart, G. J.; Farrow, B. R. H.; Healy, P. J.

doi:10.1016/s0140-6736(86)90299-0

Cited by 47 publications

(19 citation statements)

References 15 publications

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“…However, results from this and other studies suggest that early treatment for lysosomal storage diseases leads to more complete reduction of storage material in the CNS. In a canine model of fucosidosis (␣-L-fucosidase deficiency), lysosomal storage material in the CNS is reduced to a greater extent when BMT is initiated early in life (2-4 mo of age) rather than later in life (6-30 mo) (31,32). An increase in the life span, enzyme-containing donor cells in the CNS and remyelination of peripheral nerves was observed in a murine model of Krabbe's disease (galactosylceramidase deficiency) after BMT performed on 9-12-d-old animals (33,34).…”

Section: Discussionmentioning

confidence: 99%

Murine mucopolysaccharidosis type VII: long term therapeutic effects of enzyme replacement and enzyme replacement followed by bone marrow transplantation.

Sands

Vogler²,

Torrey³

et al. 1997

J. Clin. Invest.

122

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We demonstrated previously that short term administration of recombinant ␤ -glucuronidase to newborn mice with mucopolysaccharidosis type VII reduced lysosomal storage in many tissues. Lysosomal storage accumulated gradually after cessation of enzyme replacement therapy. Mice alive at 1 yr of age had decreased bone deformities and less lysosomal storage in cortical neurons. Here we compare the effects of long term enzyme replacement initiated either at birth or at 6 wk of age, and of enzyme administration initiated at birth followed by syngeneic bone marrow transplantation (BMT) at 5 wk of age. Several mice from each treatment group lived to at least 1 yr of age. Liver and spleen samples had ␤ -glucuronidase levels ranging from 2.4 to 19.8% of normal and showed a parallel decrease in lysosomal storage. The combination of enzyme replacement therapy followed by BMT reduced lysosomal distension in meninges, corneal fibroblasts, and bone when compared with treatment with enzyme alone. Mice treated at birth had less lysosomal storage in some neurons of the brain and the skeletal dysplasia was less severe when compared to mice whose treatment was delayed until 6 wk of age. We conclude that both enzyme replacement alone and early enzyme replacement followed by BMT have long term positive effects on murine mucopolysaccharidosis type VII. In addition, treatment started at birth is far more effective than treatment initiated in young adults. ( J. Clin. Invest. 1997. 1596-1605.)

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Section: Discussionmentioning

confidence: 99%

Murine mucopolysaccharidosis type VII: long term therapeutic effects of enzyme replacement and enzyme replacement followed by bone marrow transplantation.

Sands

Vogler²,

Torrey³

et al. 1997

J. Clin. Invest.

122

View full text Add to dashboard Cite

show abstract

“…6 BMT in patients or in experimental animals can lead to correction of the enzyme defect, a decrease in abnormal lysosomes in soft tisssues, and in some cases stabilisation of the neurological status. [6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] However, while there is general agreement on the effectiveness of BMT for the treatment of liver, spleen or soft tissue disease, there is no consensus on whether it has a beneficial effect on the disease induced progressive deterioration of brain function. The outcome of the neurological manifestations appears to depend on the initial mental status, the age of the patient, the engraftment of the grafted bone marrow and the development of graft-versus-host diseases (GVHD).…”

Section: Introductionmentioning

confidence: 99%

Uptake of α-(L)-iduronidase produced by retrovirally transduced fibroblasts into neuronal and glial cells in vitro

et al. 1997

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“…BMT treatment is more effective to perform before development of disease for which quick decision is required. 77,78) However, the identification of suitable donors is time consuming, 77) which is contradictory to above suggestion. Likewise, problems arise during the clinical application of gene therapy, such as difficulties in controlling the expression and localization of the enzyme, 77) and BMT is a potentially dangerous procedure.…”

Section: Treatment Of Lysosomal Storage Diseasesmentioning

confidence: 95%

“…Likewise, problems arise during the clinical application of gene therapy, such as difficulties in controlling the expression and localization of the enzyme, 77) and BMT is a potentially dangerous procedure. 79) Differences in the degree of improvement among LSD patients following treatment 70,78,[80][81][82][83] suggest the need for careful consultation prior to treatment. Enzyme replacement therapy (ERT) is the most advanced therapeutic for treating LSDs and has been applied to Gaucher disease, 61) Fabry disease, 62,63) Pompe disease, 84,85) and mucopolysaccharidosis I, 64) II 86) and VI.…”

Section: Treatment Of Lysosomal Storage Diseasesmentioning

confidence: 99%

Glycan Engineering and Production of 'Humanized' Glycoprotein in Yeast Cells

Chiba

Akeboshi

2009

Biological & Pharmaceutical Bulletin

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Protein therapeutics, such as antibodies and cytokines, is the largest class of new drug candidates being developed by pharmaceutical companies. Although most of these glycoproteins are produced in mammalian cells, there is concern that their large-scale production could be affected by an inadequate supply of bovine serum. There is also the risk of viral infection spreading through the use of contaminated protein therapeutics. Consequently, protein expression systems in yeast have been established because protein manufacturing costs are cheaper than in mammalian cells, and yeast systems are virus-free. However, yeasts cannot generate human-type glycans, and thus cannot produce therapeutic glycoproteins for human use. There has therefore been considerable interest in glycan remodeling, from yeast-type to human-type. 'Humanized' glycoproteins can now be generated in yeast by disrupting yeast-specific glycosyltransferases and introducing genes responsible for sugar-nucleotide synthesis, its transported from the cytosol to Golgi lumen, as well as their transfer and hydrolysis. A compound that inhibits yeast O-mannosyltransferase suppresses yeast-specific O-mannosyl modification, and can produce mucin-type glycoproteins. These systems are just being developed to the stage where the production in glycoengineered yeast of biopharmaceutical glycoproteins such as cytokines, antibodies for therapeutics, and enzymes for replacement therapy for lysosomal diseases are being evaluated for clinical applications. Yeast glycoprotein expression systems are expected to become the dominant approach for the production of human glycoproteins in the near future.

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Enzyme Replacement in Nervous Tissue After Allogeneic Bone-Marrow Transplantation for Fucosidosis in Dogs

Cited by 47 publications

References 15 publications

Murine mucopolysaccharidosis type VII: long term therapeutic effects of enzyme replacement and enzyme replacement followed by bone marrow transplantation.

Murine mucopolysaccharidosis type VII: long term therapeutic effects of enzyme replacement and enzyme replacement followed by bone marrow transplantation.

Uptake of α-(L)-iduronidase produced by retrovirally transduced fibroblasts into neuronal and glial cells in vitro

Glycan Engineering and Production of 'Humanized' Glycoprotein in Yeast Cells

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