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anti-Human GBA Antikörper:
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Human Polyclonal GBA Primary Antibody für ICC, IF - ABIN442242
Zancan, Bellesso, Costa, Salvalaio, Stroppiano, Hammond, Argenton, Filocamo, Moro: Glucocerebrosidase deficiency in zebrafish affects primary bone ossification through increased oxidative stress and reduced Wnt/β-catenin signaling. in Human molecular genetics 2015
This study shown GBA genetic variants for Parkinson's disease are associated with the risk of incident Parkinson's disease in the general population and with impairment in daily functioning in individuals without clinical parkinsonism.
This study showed that GBA L444P and SNCA Rep-1 were also associated with depression in Parkinson's disease.
Parkinson's disease is associated with mutations in GBA. Ashkenazi Jews GBA carriers were singled at a significantly earlier age at diagnosis compared to noncarriers.
GBA mutations are also an important risk factor for DLB development in the Spanish population, are associated with earlier disease onset, and are more prevalent in men.
Enzyme activities (acid alpha-glucosidase (GAA), galactocerebrosidase (GALC (zeige GALC Antikörper)), glucocerebrosidase (GBA), alpha-galactosidase A (GLA (zeige GLA Antikörper)), alpha-iduronidase (IDUA (zeige IDUA Antikörper)) and sphingomyeline phosphodiesterase-1 (SMPD-1 (zeige SMPD1 Antikörper))) were measured on ~43,000 de-identified dried blood spot (DBS (zeige MCF2L Antikörper)) punches, and screen positive samples were submitted for DNA sequencing to obtain genotype confirmation of disease risk
These results demonstrate the diagnostic usefulness of MLPA in the detection of GBA deletions and recombinations
A novel function for glucocerebrosidase as a regulator of sterylglucoside metabolism has been summarized. (Review)
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.
Results describe the characterization of a beta-glucosidase homolog from Arabidopsis thaliana.
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 (zeige IFNA Antikörper).
Rab7 (zeige RAB7A Antikörper) accumulated in GCase deficient cells, supporting the notion that lysosomal recycling is impaired. Since recombinant GCase can reverse ALR (zeige GFER Antikörper) 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 (zeige ABCA12 Antikörper)(-/-)) 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 (zeige SUCLA2 Antikörper)-ChlGlc-synthesizing enzyme.
Substrate compositional variation with tissue/region and Gba1 mutations in mouse models--implications for Gaucher disease.
GBA1 and GBA2 (zeige GBA2 Antikörper) 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.
, acid beta-glucosidase
, lysosomal glucocerebrosidase
, acid beta glucosidase
, glucosidase, beta; acid
, glucosidase, beta, acid
, glucosidase, beta; acid (includes glucosylceramidase)