HIV TAT variants differentially influence the production of glucocerebrosidase in Sf9 cells
Genet. mol. res. (Online)
;
4(3): 491-495, 2005. ilus
Artigo
em Inglês
| 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.
Texto completo:
DisponíveL
Índice:
LILACS (Américas)
Assunto principal:
Produtos do Gene tat
/
Glucosilceramidase
Limite:
Humanos
Idioma:
Inglês
Revista:
Genet. mol. res. (Online)
Assunto da revista:
Biologia Molecular
/
Genética
Ano de publicação:
2005
Tipo de documento:
Artigo
País de afiliação:
Canadá
Instituição/País de afiliação:
University of Calgary/CA
/
University of Victoria/CA
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