| Dystonia as initial presentation of compound heterozygous GBA2 mutations: Expanding the phenotypic spectrum of SPG46. | Dystonia as initial presentation of compound heterozygous GBA2 mutations: Expanding the phenotypic spectrum of SPG46.
Kloth K, Cozma C, Bester M, Gerloff C, Biskup S, Zittel S. | 04/3/2021 |
| Truncated mutants of beta-glucosidase 2 (GBA2) are localized in the mitochondrial matrix and cause mitochondrial fragmentation. | Truncated mutants of beta-glucosidase 2 (GBA2) are localized in the mitochondrial matrix and cause mitochondrial fragmentation.
Sultana S, Stewart J, van der Spoel AC., Free PMC Article | 08/22/2020 |
| 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 |
| We conclude that the c.1780G>C mutation results in NLGase loss of function with abolishment of the enzymatic activity and accumulation of GlcCer accompanied by a compensatory increase in GCase. | Biochemical Characterization of the GBA2 c.1780G>C Missense Mutation in Lymphoblastoid Cells from Patients with Spastic Ataxia.
Malekkou A, Samarani M, Drousiotou A, Votsi C, Sonnino S, Pantzaris M, Chiricozzi E, Zamba-Papanicolaou E, Aureli M, Loberto N, Christodoulou K., Free PMC Article | 01/19/2019 |
| 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. | Evidence for the Involvement of Lipid Rafts and Plasma Membrane Sphingolipid Hydrolases in Pseudomonas aeruginosa Infection of Cystic Fibrosis Bronchial Epithelial Cells.
Schiumarini D, Loberto N, Mancini G, Bassi R, Giussani P, Chiricozzi E, Samarani M, Munari S, Tamanini A, Cabrini G, Lippi G, Dechecchi MC, Sonnino S, Aureli M., Free PMC Article | 09/1/2018 |
| 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 | Novel mutations in genes causing hereditary spastic paraplegia and Charcot-Marie-Tooth neuropathy identified by an optimized protocol for homozygosity mapping based on whole-exome sequencing.
Kancheva D, Atkinson D, De Rijk P, Zimon M, Chamova T, Mitev V, Yaramis A, Maria Fabrizi G, Topaloglu H, Tournev I, Parman Y, Parma Y, Battaloglu E, Estrada-Cuzcano A, Jordanova A. | 12/16/2017 |
| GBA mutations as risk factors for PD and point to lysosomal dysfunction as a mechanism contributing to PD etiology. | Strong association between glucocerebrosidase mutations and Parkinson's disease in Sweden.
Ran C, Brodin L, Forsgren L, Westerlund M, Ramezani M, Gellhaar S, Xiang F, Fardell C, Nissbrandt H, Söderkvist P, Puschmann A, Ygland E, Olson L, Willows T, Johansson A, Sydow O, Wirdefeldt K, Galter D, Svenningsson P, Belin AC., Free PMC Article | 10/21/2017 |
| GBA2 mutations causing a Marinesco-Sjogren-like syndrome in two Norwegian families, are reported. | GBA2 Mutations Cause a Marinesco-Sjögren-Like Syndrome: Genetic and Biochemical Studies.
Haugarvoll K, Johansson S, Rodriguez CE, Boman H, Haukanes BI, Bruland O, Roque F, Jonassen I, Blomqvist M, Telstad W, Månsson JE, Knappskog PM, Bindoff LA., Free PMC Article | 08/12/2017 |
| Mutagenic analysis of TxGH116 and structural modeling of GBA2 provide a detailed structural and functional rationale for pathogenic missense mutations of GBA2 | Bacterial β-Glucosidase Reveals the Structural and Functional Basis of Genetic Defects in Human Glucocerebrosidase 2 (GBA2).
Charoenwattanasatien R, Pengthaisong S, Breen I, Mutoh R, Sansenya S, Hua Y, Tankrathok A, Wu L, Songsiriritthigul C, Tanaka H, Williams SJ, Davies GJ, Kurisu G, Cairns JR., Free PMC Article | 07/8/2017 |
| 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 |
| The results suggested that SPG46 and SPG56 are rare causes of hereditary spastic paraplegia in China. | SPG46 and SPG56 are rare causes of hereditary spastic paraplegia in China.
Yang YJ, Zhou ZF, Liao XX, Luo YY, Zhan ZX, Huang MF, Zhou L, Tang BS, Shen L, Du J. | 04/8/2017 |
| Spastic paraplegia/cerebellar ataxia patients have a severe deficit in GBA2 activity, because the GBA2 mutants are intrinsically inactive and/or reduced in amount. | Lack of enzyme activity in GBA2 mutants associated with hereditary spastic paraplegia/cerebellar ataxia (SPG46).
Sultana S, Reichbauer J, Schüle R, Mochel F, Synofzik M, van der Spoel AC. | 11/28/2015 |
| 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 | A new locus (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.
Boukhris A, Feki I, Elleuch N, Miladi MI, Boland-Augé A, Truchetto J, Mundwiller E, Jezequel N, Zelenika D, Mhiri C, Brice A, Stevanin G. | 11/29/2014 |
| The GBA2 gene shows a low mutation frequency in a general population of complicated hereditary spastic paraparesis | Mutations in CYP2U1, DDHD2 and GBA2 genes are rare causes of complicated forms of hereditary spastic paraparesis.
Citterio A, Arnoldi A, Panzeri E, D'Angelo MG, Filosto M, Dilena R, Arrigoni F, Castelli M, Maghini C, Germiniasi C, Menni F, Martinuzzi A, Bresolin N, Bassi MT. | 10/4/2014 |
| Whole-exome and targeted sequencing have defined the genetic basis of dizziness including new genes causing ataxia: GBA2, TGM6, ANO10 and SYT14 | Genetics of dizziness: cerebellar and vestibular disorders.
Requena T, Espinosa-Sanchez JM, Lopez-Escamez JA. | 08/16/2014 |
| 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. | A novel GBA2 gene missense mutation in spastic ataxia.
Votsi C, Zamba-Papanicolaou E, Middleton LT, Pantzaris M, Christodoulou K. | 08/9/2014 |
| observations make GBA2 a likely candidate to be involved in Gaucher disease etiology. | Functional and genetic characterization of the non-lysosomal glucosylceramidase 2 as a modifier for Gaucher disease.
Yildiz Y, Hoffmann P, Vom Dahl S, Breiden B, Sandhoff R, Niederau C, Horwitz M, Karlsson S, Filocamo M, Elstein D, Beck M, Sandhoff K, Mengel E, Gonzalez MC, Nöthen MM, Sidransky E, Zimran A, Mattheisen M., Free PMC Article | 07/19/2014 |
| 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 |
| This study suggests GBA2 mutations are a cause of recessive spastic ataxia and responsible for a form of glucosylceramide storage disease in humans. | Mutations in GBA2 cause autosomal-recessive cerebellar ataxia with spasticity.
Hammer MB, Eleuch-Fayache G, Schottlaender LV, Nehdi H, Gibbs JR, Arepalli SK, Chong SB, Hernandez DG, Sailer A, Liu G, Mistry PK, Cai H, Shrader G, Sassi C, Bouhlal Y, Houlden H, Hentati F, Amouri R, Singleton AB., Free PMC Article | 04/6/2013 |
| GBA2 loss of function led to abnormal motor behavior and axonal shortening/branching of motoneurons. | Loss of function of glucocerebrosidase GBA2 is responsible for motor neuron defects in hereditary spastic paraplegia.
Martin E, Schüle R, Smets K, Rastetter A, Boukhris A, Loureiro JL, Gonzalez MA, Mundwiller E, Deconinck T, Wessner M, Jornea L, Oteyza AC, Durr A, Martin JJ, Schöls L, Mhiri C, Lamari F, Züchner S, De Jonghe P, Kabashi E, Brice A, Stevanin G., Free PMC Article | 04/6/2013 |
| 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 |
| GBA2 is down-regulated in melanoma; inducible expression of GBA2 affects endogenous sphingolipid metabolism by promoting glucosylceramide degradation (decrease by 78%) and ceramide generation. | The nonlysosomal β-glucosidase GBA2 promotes endoplasmic reticulum stress and impairs tumorigenicity of human melanoma cells.
Sorli SC, Colié S, Albinet V, Dubrac A, Touriol C, Guilbaud N, Bedia C, Fabriàs G, Casas J, Ségui B, Levade T, Andrieu-Abadie N. | 03/30/2013 |
| 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 |
| Results describe the association between the MTX1 and beta-glucocerebrosidase genes and its possible effect on Parkinson disease. | Homozygosity for the MTX1 c.184T>A (p.S63T) alteration modifies the age of onset in GBA-associated Parkinson's disease.
Gan-Or Z, Bar-Shira A, Gurevich T, Giladi N, Orr-Urtreger A. | 03/31/2012 |
| The structure of the N370S acid-beta-glucosidase mutant that causes Gaucher disease was studied. | Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-beta-glucosidase mutant that causes Gaucher disease.
Offman MN, Krol M, Rost B, Silman I, Sussman JL, Futerman AH. | 12/31/2011 |