HIV TAT variants differentially influence the production of glucocerebrosidase in Sf9 cells
Genet. mol. res. (Online)
;
4(3): 491-495, 2005. ilus
Article
in English
| LILACS
| ID: lil-444963
ABSTRACT
Gaucher disease, the most common lysosomal storage disorder, is currently treated with enzyme replacement therapy. This approach, however, is ineffective in altering the progression of neurodegeneration in type 2 and type 3 patients due to the difficulty of transferring the recombinant enzyme across the blood-brain barrier. Human immunodeficiency virus type 1 trans-activating transcriptional activator protein (HIV TAT) contains a protein transduction domain that can be added to a fusion protein partner to allow for transport of the partner across membranes. Consequently, we examined the creation, production, and secretion of fusion constructs containing glucocerebrosidase and either wild-type TAT or modified TAT in Sf9 cells. All three constructs exhibited successful expression, with wild-type TAT chimeras showing lower levels of expression than modified TAT chimeras.
Full text:
Available
Index:
LILACS (Americas)
Main subject:
Gene Products, tat
/
Glucosylceramidase
Limits:
Humans
Language:
English
Journal:
Genet. mol. res. (Online)
Journal subject:
Molecular Biology
/
Genetics
Year:
2005
Type:
Article
Affiliation country:
Canada
Institution/Affiliation country:
University of Calgary/CA
/
University of Victoria/CA
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