| In heterozygous GBA1 mutant mice, there was also significantly reduced GBA2 GCase enzyme activity specifically within the hippocampus. Such reductions in GBA2 GCase enzyme could contribute to the pathological and behavioural effects seen. | Age-related neurochemical and behavioural changes in D409V/WT GBA1 mouse: Relevance to lewy body dementia.
Clarke E, Jantrachotechatchawan C, Buhidma Y, Broadstock M, Yu L, Howlett D, Aarsland D, Ballard C, Francis PT. | 05/16/2020 |
| results shed light on the molecular mechanism underlying the pathogenesis of GBA2-related hereditary spastic paraplegia (HSP), autosomal-recessive cerebellar ataxia (ARCA) and reveal species-specific differences in GBA2 function in vivo | Species-specific differences in nonlysosomal glucosylceramidase GBA2 function underlie locomotor dysfunction arising from loss-of-function mutations.
Woeste MA, Stern S, Raju DN, Grahn E, Dittmann D, Gutbrod K, Dörmann P, Hansen JN, Schonauer S, Marx CE, Hamzeh H, Körschen HG, Aerts JMFG, Bönigk W, Endepols H, Sandhoff R, Geyer M, Berger TK, Bradke F, Wachten D., Free PMC Article | 06/1/2019 |
| sphingosine, the cytotoxic metabolite accumulating in Gaucher cells through the action of GBA2, directly binds to GBA2 and inhibits its activity. | Identification of a feedback loop involving β-glucosidase 2 and its product sphingosine sheds light on the molecular mechanisms in Gaucher disease.
Schonauer S, Körschen HG, Penno A, Rennhack A, Breiden B, Sandhoff K, Gutbrod K, Dörmann P, Raju DN, Haberkant P, Gerl MJ, Brügger B, Zigdon H, Vardi A, Futerman AH, Thiele C, Wachten D., Free PMC Article | 04/29/2017 |
| GBA2 is particularly abundant in Purkinje cells (PCs), one of the most affected neuronal populations in NPC disease. | Reducing GBA2 Activity Ameliorates Neuropathology in Niemann-Pick Type C Mice.
Marques AR, Aten J, Ottenhoff R, van Roomen CP, Herrera Moro D, Claessen N, Vinueza Veloz MF, Zhou K, Lin Z, Mirzaian M, Boot RG, De Zeeuw CI, Overkleeft HS, Yildiz Y, Aerts JM., Free PMC Article | 05/7/2016 |
| glucosylceramide accumulation in GBA2 knockout-mice alters cytoskeletal dynamics due to a more ordered lipid organization in the plasma membrane. Similar cytoskeletal defects were observed in male germ and Sertoli cells from GBA2 knockout-mice. | Accumulation of glucosylceramide in the absence of the beta-glucosidase GBA2 alters cytoskeletal dynamics.
Raju D, Schonauer S, Hamzeh H, Flynn KC, Bradke F, Vom Dorp K, Dörmann P, Yildiz Y, Trötschel C, Poetsch A, Breiden B, Sandhoff K, Körschen HG, Wachten D., Free PMC Article | 01/2/2016 |
| the deletion of Gba2 significantly rescues the type 1 Gaucher disease clinical phenotype. | Glucocerebrosidase 2 gene deletion rescues type 1 Gaucher disease.
Mistry PK, Liu J, Sun L, Chuang WL, Yuen T, Yang R, Lu P, Zhang K, Li J, Keutzer J, Stachnik A, Mennone A, Boyer JL, Jain D, Brady RO, New MI, Zaidi M., Free PMC Article | 06/7/2014 |
| redefine GBA2 activity as the beta-glucosidase that is sensitive to inhibition by N-butyldeoxygalactonojirimycin. | β-Glucosidase 2 (GBA2) activity and imino sugar pharmacology.
Ridley CM, Thur KE, Shanahan J, Thillaiappan NB, Shen A, Uhl K, Walden CM, Rahim AA, Waddington SN, Platt FM, van der Spoel AC., Free PMC Article | 02/8/2014 |
| GBA2 is localized at the ER and Golgi, which puts GBA2 in a key position for a lysosome-independent route of glucosylceramide-dependent signaling. | The non-lysosomal β-glucosidase GBA2 is a non-integral membrane-associated protein at the endoplasmic reticulum (ER) and Golgi.
Körschen HG, Yildiz Y, Raju DN, Schonauer S, Bönigk W, Jansen V, Kremmer E, Kaupp UB, Wachten D., Free PMC Article | 03/30/2013 |
| The repression of IL-6/STAT3 signalling pathway seems to be one of the mechanisms for the delay of liver regeneration in GBA2-deficient mice. | Beta-glucosidase 2 knockout mice with increased glucosylceramide show impaired liver regeneration.
Gonzalez-Carmona MA, Sandhoff R, Tacke F, Vogt A, Weber S, Canbay AE, Rogler G, Sauerbruch T, Lammert F, Yildiz Y. | 01/26/2013 |
| GBA1 and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples. | Beta-glucosidase 1 (GBA1) is a second bile acid β-glucosidase in addition to β-glucosidase 2 (GBA2). Study in β-glucosidase deficient mice and humans.
Harzer K, Blech-Hermoni Y, Goldin E, Felderhoff-Mueser U, Igney C, Sidransky E, Yildiz Y., Free PMC Article | 09/22/2012 |
| The coiled-coil structure of LIMP-2 is required for its interaction with beta-glucocerebrosidase. | Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase.
Blanz J, Groth J, Zachos C, Wehling C, Saftig P, Schwake M. | 04/12/2010 |
| L-type calcium channel blockers have the ex vivo effects of increasing GCase activity and protein in mouse fibroblasts | In vivo and ex vivo evaluation of L-type calcium channel blockers on acid beta-glucosidase in Gaucher disease mouse models.
Sun Y, Liou B, Quinn B, Ran H, Xu YH, Grabowski GA., Free PMC Article | 03/15/2010 |
| testis GBA2 is present in both somatic and germ cells | Accumulation of glucosylceramide in murine testis, caused by inhibition of beta-glucosidase 2: implications for spermatogenesis.
Walden CM, Sandhoff R, Chuang CC, Yildiz Y, Butters TD, Dwek RA, Platt FM, van der Spoel AC. | 01/21/2010 |
| GBA2 is a glucosylceramidase whose loss causes accumulation of glycolipids and an endoplasmic reticulum storage disease | Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility.
Yildiz Y, Matern H, Thompson B, Allegood JC, Warren RL, Ramirez DM, Hammer RE, Hamra FK, Matern S, Russell DW., Free PMC Article | 01/21/2010 |
| the non-lysosomal glucosylceramidase is identical to the earlier described bile acid beta-glucosidase, being beta-glucosidase 2 | Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2.
Boot RG, Verhoek M, Donker-Koopman W, Strijland A, van Marle J, Overkleeft HS, Wennekes T, Aerts JM. | 01/21/2010 |