HIV TAT variants differentially influence the production of glucocerebrosidase in Sf9 cells.
Genet Mol Res
; 4(3): 491-5, 2005 Sep 30.
Article
em En
| MEDLINE
| ID: mdl-16342033
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.
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Base de dados:
MEDLINE
Assunto principal:
Produtos do Gene tat
/
Glucosilceramidase
Limite:
Humans
Idioma:
En
Ano de publicação:
2005
Tipo de documento:
Article