title: HIV TAT variants differentially influence the production of glucocerebrosidase in Sf9 cells.
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.
authors.affiliation: Department of Biology, University of Victoria, Victoria, BC, Canada.
authors.forename: Andrea K
authors.initials: AK
authors.lastname: Vaags
authors.forename: Tessa N
authors.initials: TN
authors.lastname: Campbell
authors.forename: Francis Y M
authors.initials: FY
authors.lastname: Choy
mesh_terms: D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D005776:Gaucher Disease / Q000378:metabolism / Q000628:therapy; D015696:Gene Products, tat / Q000235:genetics / Q000378:metabolism*; D005962:Glucosylceramidase / Q000096:biosynthesis* / Q000235:genetics; D006801:Humans; D021381:Protein Transport / Q000235:genetics; D014158:Transcription, Genetic; D014161:Transduction, Genetic
chemical_list: D015696:Gene Products, tat; D005962:Glucosylceramidase