Gba Antibody, Biotin conjugated

1. Thus, while the underlying mechanism is not clear, this model shows that gba deficiency impacts the age of onset and disease duration in aged SNCA(A53T) mice, providing a valuable resource to identify modifiers, pathways and possible moonlighting roles of glucocerebrosidase in Parkinson pathogenesis. PMID:29173981
2. The data support the contention that prolonged antagonism of glucosylceramide synthase (GCS)in the central nervous system (CNS)can affect alpha-synuclein processing and improve behavioral outcomes. Hence, inhibition of GCS represents a disease-modifying therapeutic strategy for GBA-related synucleinopathies and conceivably for certain forms of sporadic disease PMID:28223512
3. These results indicate that Gba1 deficiency enhances neuronal vulnerability to neurodegenerative processes triggered by increased alpha-synuclein expression. PMID:28969384
4. This study demonstrated that the gba1 deficiency mice showed gene regulation expression of the type I interferon. PMID:27175482
5. Rab7 accumulated in GCase deficient cells, supporting the notion that lysosomal recycling is impaired. Since recombinant GCase can reverse ALR impairment, we anticipate that strategies to restore GCase activity in the brains of both sporadic patients with PD and those with GBA1 mutations will improve autophagy lysosomal pathway, preventing the accumulation of a-synuclein and spread of pathology. PMID:27378698
6. heterozygosity for a Gaucher disease-associated mutation in glucocerebrosidase interferes with alpha-synuclein degradation and contributes to its accumulation PMID:25351739
7. Data indicate that ABC transporter A family member 12 knockout (Abca12(-/-)) epidermis had 5-fold more beta-glucocerebrosidase (GCase) protein, and a 5-fold increase in GCase activity. PMID:24293640
8. These results demonstrate, for the first time, a novel function of GBA1 as a beta-ChlGlc-synthesizing enzyme. PMID:24211208
9. Substrate compositional variation with tissue/region and Gba1 mutations in mouse models--implications for Gaucher disease. PMID:23520473
10. GBA1 and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples. PMID:22659419
11. results not only point to a fundamental role for GBA in immune regulation but also suggest that GBA mutations in GD may cause widespread immune dysregulation through the accumulation of substrates PMID:22665763
12. This study suggested that several leads connecting GBA1 mutations with alpha-synuclein misprocessing have emerged as potential targets for the treatment of GBA1-related synucleinopathies. PMID:22327140
13. IFG stabilizes GCase in tissues and serum and can reduce visceral substrates in vivo. PMID:22167193
14. Mutations in GBA1 can cause Parkinson disease-like alpha-synuclein pathology; rescuing brain glucocerebrosidase activity might represent a therapeutic strategy for GBA1-associated synucleinopathies. PMID:21730160
15. evidence for the involvement of deletion of the GBA1 gene in multiple cell lineages in nonneuronopathic type 1 Gaucher disease PMID:20962279
16. The saposin C deficient mice backcrossed to point mutated GCase mimics the central nervous system phenotype and biochemistry of some type 3 (neuronopathic) variants of Gaucher disease. PMID:20047948
17. isofagomine increases the activity of the Gaucher disease L444P mutant form of beta-glucosidase PMID:20148966
18. Saposin C has multiple roles in glycosphingolipid catabolism and functions in Central Nervous System independent of its role as an stabilizer of GCase. PMID:20015957
19. mRNA shows generalized low level expression early in gestation with gradual appearance of differential expression appearing around gestational age E14 and significantly increasing at term and into adulthood. PMID:11749048
20. Results indicate that glucocerebrosidase deficiency, even in the absence of large amounts of sphingolipid storage, can trigger an inflammatory reaction. PMID:11994410
21. data indicate that saposin C is required for acid beta-glucosidase resistance to proteolytic degradation in the cell PMID:12813057

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UNIGENE: Mm.5031

KEGG: mmu:14466

STRING: 10090.ENSMUSP00000076589