Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

By cellular hybridization with C11D cells, the following gene assignments to specific chromosomes were demonstrated for the chimpanzee: beta-glucuronidase on chromosome 7, enolase-2 on chromosome 12, and the phosphoglycerate kinase on the X.
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PMID:[Assignment of the genes of beta-glucuronidase, enolase-2 and phosphoglycerate kinase to chromosomes 7, 12 and X in the Chimpanzee]. 30 52

Sl, Sld, and Slt are mutant alleles at the steel locus. All Sl/Sld and most Sl/Slt female mice are infertile, but the cause of the infertility is different. Germ cells are absent in Sl/Sld ovaries but present in Sl/Slt ovaries. The infertility of Sl/Slt female mice was attributed to the growth arrest of ovarian follicles, and the mechanism was analyzed by producing aggregation chimeras between Sl/Slt and +/+ embryos. Sl/Slt oocytes were ovulated and fertilized in Sl/Slt----+/+ chimeras. We investigated the origin of granulosa cells in the growing follicles and that of granulosa-derived luteal cells in the chimeras by using the electrophoretic pattern of phosphoglycerate kinase-1 and the histochemical activity of beta-glucuronidase as markers. Granulosa cells of Sl/Slt genotype developed and constituted pregnant corpora lutea in Sl/Slt----+/+ chimeras. Therefore, the growth arrest of Sl/Slt ovarian follicles may not be due to an intrinsic defect in granulosa cells but may instead be due to an intrinsic defect in ovarian stromal cells. This suggests that normal stromal cells are essential for the development of ovarian follicles.
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PMID:Infertility due to growth arrest of ovarian follicles in Sl/Slt mice. 334 38

Genetic defects of lysosomal hydrolases result in severe storage diseases and treatments based on enzyme replacement have been proposed. In mice lacking beta-glucuronidase, which develop a disease homologous to human mucopolysaccharidosis type VII (MPS VII, sly syndrome), we have used autologous implants of genetically-modified cells for the continuous in vivo production of the enzyme. A retroviral vector containing the human beta-glucuronidase cDNA under the control of the mouse phosphoglycerate kinase promoter was used to infect primary skin fibroblasts, bone marrow cells, or myoblasts from mutant MPS VII animals. The fibroblasts were embedded into collagen lattices and reimplanted into the peritoneal cavity of recipient MPS VII mice. All animals, when analysed 10 to 155 days later, expressed beta-glucuronidase from the vascularised neo-organs that developed after implantation, and accumulated the enzyme in their tissues. A complete disappearance of the lysosomal storage lesions was observed in their liver and spleen. This procedure has been scaled up for long term lysosomal enzyme delivery in dogs. The bone marrow cells were used for partial hematopoietic reconstruction of sublethally irradiated MPS VII mice. Five months after gene transfer, animals in which under 5% of genetically-modified hematopoietic cells were detected in the spleen showed a drastic reduction of lysosomal storage lesions in the liver and spleen. Genetically-modified myoblasts were transplanted into injured muscles, where they participated in the regeneration of a significant proportion of muscle fibers. Enzyme secretion and liver uptake were observed for at least one month.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Gene therapy for lysosomal disorders. 817 9

Glycosomal phosphoglycerate kinase (gPGK) of Trypanosoma brucei differs from the cytoplasmic isozyme (cPGK) in its higher isoelectric point characterized by clusters of positive charges along the polypeptide chain, and a 20 amino acid C-terminal extension ending in serine-serine-leucine (SSL). While a C-terminal SSL tripeptide is apparently not capable of directing luciferase to the peroxisomes in mammalian cells [J. Cell Biol. 108 (1989), 1657-1664], we show here that it is sufficient for the import of luciferase as well as an unrelated protein, beta-glucuronidase, into the glycosomes of T. brucei, as determined by immunoelectron microscopy. The analysis of luciferase-gPGK fusion proteins indicates that the only targeting signal for import of gPGK into the glycosome resides in this C-terminal SSL sequence.
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PMID:The C-terminal tripeptide of glycosomal phosphoglycerate kinase is both necessary and sufficient for import into the glycosomes of Trypanosoma brucei. 842 38