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Results describe the characterization of a beta-glucosidase homolog from Arabidopsis thaliana.
Mutant GBA proteins cause increases in alpha-synuclein levels, while an inhibition of GBA by alpha-synuclein has been also demonstrated in Gaucher disease patients with Parkinson disease. (Review)
GBA mutations as risk factors for PD and point to lysosomal dysfunction as a mechanism contributing to PD etiology.
Parkinson patient who carry mutations in the GBA gene demonstrates more significant cognitive decline compared to idiopathic parkinson patients.
Mesenchymal stem cells with reduced GBA activity are prone to apoptosis and senescence due to impaired autophagy and DNA repair capacity.
Local lysosomal conditions may be even more critical for some mutant lysosomal hydrolases, e.g. for mutant GBA1 . In Niemann-Pick disease type C disease, characterized by the cholesterol primary storage, GlcCer secondary accumulation could be triggered by SM secondary accumulation.
the GBA1 gene, its role in Gaucher disease, and its link with Parkinson disease (Review)
the decrease in enzymatic activity of lysosomal hydrolases in GBA mutation carriers may contribute to Parkinson disease pathogenesis by increasing the level of neurotoxic oligomeric alpha-synuclein species.
the important contribution of GBA (L444P and N370S) mutations to parkinsonism in Brazilian families.
In a Flanders-Belgian cohort, carrier status of a heterozygous glucocerebrosidase (GBA) mutation was a strong genetic risk factor for Parkinson's disease (PD). The GBA mutation frequency of 4.5% is comparable to previously reported data in other European PD patient cohorts.
Rab7 (show RAB7B Proteins) accumulated in GCase deficient cells, supporting the notion that lysosomal recycling is impaired. Since recombinant GCase can reverse ALR (show GFER Proteins) 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.
These results indicate that Gba1 deficiency enhances neuronal vulnerability to neurodegenerative processes triggered by increased alpha-synuclein expression.
This study demonstrated that the gba1 deficiency mice showed gene regulation expression of the type I interferon (show IFNA Proteins).
Rab7 (show RAB7A Proteins) accumulated in GCase deficient cells, supporting the notion that lysosomal recycling is impaired. Since recombinant GCase can reverse ALR (show GFER Proteins) 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.
In LIMP-2-deficient brains a significant reduction in GC activity led to lipid storage, disturbed autophagic/lysosomal function, and alpha-synuclein accumulation.
heterozygosity for a Gaucher disease-associated mutation in glucocerebrosidase interferes with alpha-synuclein degradation and contributes to its accumulation
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.
These results demonstrate, for the first time, a novel function of GBA1 as a beta (show SUCLA2 Proteins)-ChlGlc-synthesizing enzyme.
Substrate compositional variation with tissue/region and Gba1 mutations in mouse models--implications for Gaucher disease.
GBA1 and GBA2 (show GBA2 Proteins) activities had characteristic differences between the studied fibroblast, liver and brain samples.
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
genetic analysis and mapping of the porcine glucocerebrosidase (GBA) gene
This gene encodes a lysosomal membrane protein that cleaves the beta-glucosidic linkage of glycosylceramide, an intermediate in glycolipid metabolism. Mutations in this gene cause Gaucher disease, a lysosomal storage disease characterized by an accumulation of glucocerebrosides. A related pseudogene is approximately 12 kb downstream of this gene on chromosome 1. Alternative splicing results in multiple transcript variants.
, glucosidase, beta, acid
, D-glucosyl-N-acylsphingosine glucohydrolase
, acid beta-glucosidase
, lysosomal glucocerebrosidase
, acid beta glucosidase
, glucosidase, beta; acid (includes glucosylceramidase)
, glucosidase, beta; acid