Recombinant Human Non-lysosomal glucosylceramidase (GBA2), partial

1. Demonstrate that GBA2 plays a role in the proinflammatory state characterizing cystic fibrosis cells. Report for the first time that Pseudomonas aeruginosa infection causes a recruitment of plasma membrane-associated glycosphingolipid hydrolases into lipid rafts of CuFi-1-infected cells. PMID: 29333001
2. Our protocol showed high specificity and sensitivity for homozygosity detection and facilitated the identification of novel mutations in GAN, GBA2, and ZFYVE26 in four families affected by hereditary spastic paraplegia or Charcot-Marie-Tooth disease PMID: 26492578
3. GBA mutations as risk factors for PD and point to lysosomal dysfunction as a mechanism contributing to PD etiology. PMID: 27255555
4. GBA2 mutations causing a Marinesco-Sjogren-like syndrome in two Norwegian families, are reported. PMID: 28052128
5. Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2 PMID: 27115290
6. sphingosine, the cytotoxic metabolite accumulating in Gaucher cells through the action of GBA2, directly binds to GBA2 and inhibits its activity. PMID: 28258214
7. The results suggested that SPG46 and SPG56 are rare causes of hereditary spastic paraplegia in China. PMID: 27553021
8. Spastic paraplegia/cerebellar ataxia patients have a severe deficit in GBA2 activity, because the GBA2 mutants are intrinsically inactive and/or reduced in amount. PMID: 26220345
9. SPG46 maps to 9p21.2-q21.12 in a Tunisian family with a complicated autosomal recessive hereditary spastic paraplegia with mental impairment and thin corpus callosum PMID: 20593214
10. The GBA2 gene shows a low mutation frequency in a general population of complicated hereditary spastic paraparesis PMID: 24337409
11. We hereby report a novel GBA2 mutation associated with spastic ataxia and suggest that GBA2 mutations may be a relatively frequent cause of autosomal recessive cerebellar ataxias. PMID: 24252062
12. observations make GBA2 a likely candidate to be involved in Gaucher disease etiology. PMID: 24070122
13. redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin. PMID: 23880767
14. GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons. PMID: 23332916
15. This study suggests GBA2 mutations are a cause of recessive spastic ataxia and responsible for a form of glucosylceramide storage disease in humans. PMID: 23332917
16. GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling. PMID: 23250757
17. GBA2 is down-regulated in melanoma; inducible expression of GBA2 affects endogenous sphingolipid metabolism by promoting glucosylceramide degradation (decrease by 78%) and ceramide generation. PMID: 23073830
18. GBA1 and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples. PMID: 22659419
19. Results describe the association between the MTX1 and beta-glucocerebrosidase genes and its possible effect on Parkinson disease. PMID: 21837367
20. The structure of the N370S acid-beta-glucosidase mutant that causes Gaucher disease was studied. PMID: 21724649
21. Beta-glycosidase from Sulfolobus solfataricus shows distant similarity to the non-lysosomal bile acid beta-glucosidase GBA2 in humans. PMID: 20427274
22. Action Myoclonus-Renal Failure Syndrome-causing mutations within LIMP-2 affect the binding to beta-glucocerebrosidase. PMID: 19933215
23. the non-lysosomal glucosylceramidase is identical to the earlier described bile acid beta-glucosidase, being beta-glucosidase 2 PMID: 17105727
24. This study suggested that glucosidase-beta variants have a limited role in susceptibility to Lewy body disease in North America. PMID: 18829375

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HGNC: 18986

OMIM: 609471

KEGG: hsa:57704

STRING: 9606.ENSP00000367343

UniGene: Hs.443134