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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Glucosidase, beta

bile acid beta-glucosidase, GBA2, beta-glucosidase 2, non-lysosomal glucosylceramidase
This gene encodes a microsomal beta-glucosidase that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. Studies to determine subcellular localization of this protein in the liver indicated that the enzyme was mainly enriched in the microsomal fraction where it appeared to be confined to the endoplasmic reticulum. This putative transmembrane protein is thought to play a role in carbohydrate transport and metabolism. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, gBa, CAN, HAD, GCS
Papers on bile acid beta-glucosidase
Glucosylated cholesterol in mammalian cells and tissues: formation and degradation by multiple cellular β-glucosidases.
Aerts et al., Netherlands. In J Lipid Res, Feb 2016
Cells express two GlcCer-degrading β-glucosidases, GBA and GBA2, located in and outside the lysosome, respectively.
ALS5/SPG11/KIAA1840 mutations cause autosomal recessive axonal Charcot-Marie-Tooth disease.
Orlacchio et al., Roma, Italy. In Brain, Jan 2016
Besides, we screened for all the known genes related to axonal autosomal recessive Charcot-Marie-Tooth disease (CMT2A2/HMSN2A2/MFN2, CMT2B1/LMNA, CMT2B2/MED25, CMT2B5/NEFL, ARCMT2F/dHMN2B/HSPB1, CMT2K/GDAP1, CMT2P/LRSAM1, CMT2R/TRIM2, CMT2S/IGHMBP2, CMT2T/HSJ1, CMTRID/COX6A1, ARAN-NM/HINT and GAN/GAN), for the genes related to autosomal recessive hereditary spastic paraplegia with thin corpus callosum and axonal peripheral neuropathy (SPG7/PGN, SPG15/ZFYVE26, SPG21/ACP33, SPG35/FA2H, SPG46/GBA2, SPG55/C12orf65 and SPG56/CYP2U1), as well as for the causative gene of peripheral neuropathy with or without agenesis of the corpus callosum (SLC12A6).
Synthesis and Evaluation of Hybrid Structures Composed of Two Glucosylceramide Synthase Inhibitors.
Aerts et al., Leiden, Netherlands. In Chemmedchem, Dec 2015
Selective modulation of one of the glycoprocessing enzymes involved in glucosylceramide metabolism-glucosylceramide synthase (GCS), acid glucosylceramidase (GBA1), or neutral glucosylceramidase (GBA2)-is therefore an attractive research objective.
Current and Novel Aspects on the Non-lysosomal β-Glucosylceramidase GBA2.
Sandro et al., Milano, Italy. In Neurochem Res, Dec 2015
UNASSIGNED: The non-lysosomal β-glucosylceramidase GBA2 (EC3.2.1.45,
Glucosylceramidases and malignancies in mammals.
Levade et al., Toulouse, France. In Biochimie, Dec 2015
GBA2 is a ubiquitous non-lysosomal glucosylceramidase whose mutations have been associated with some forms of hereditary spastic paraplegia.
High β-glucosidase (GBA) activity not attributable to GBA1 and GBA2 in live normal and enzyme-deficient fibroblasts may emphasise the role of additional GBAs.
Yildiz et al., In Biol Chem, Nov 2015
Beta-glucosidases (GBA) include GBA1, GBA2 and other β-glucosidases (non-GBA1-2).
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.
Jordanova et al., Antwerp, Belgium. In Genet Med, Nov 2015
RESULTS: 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.
Lack of enzyme activity in GBA2 mutants associated with hereditary spastic paraplegia/cerebellar ataxia (SPG46).
van der Spoel et al., Halifax, Canada. In Biochem Biophys Res Commun, Oct 2015
Glucosylceramide is degraded to ceramide and glucose by distinct, non-homologous enzymes, including glucocerebrosidase (GBA), localized in the endolysosomal pathway, and β-glucosidase 2 (GBA2), which is associated with the plasma membrane and/or the endoplasmic reticulum.
Different pediatric brain tumors are associated with different gene expression profiling.
Malaguarnera et al., Catania, Italy. In Acta Histochem, May 2015
In addition evaluating other lisosomal enzymes such as glycosidases and proteases we found that NEU4, CTBS and GBA2 belonging to glycosidases family and CTSC, CTSK and CTSF belonging to proteases family were differently modulated.
Accumulation of glucosylceramide in the absence of the beta-glucosidase GBA2 alters cytoskeletal dynamics.
Wachten et al., Bonn, Germany. In Plos Genet, Mar 2015
Here, we reveal that glucosylceramide accumulation in GBA2 knockout-mice alters cytoskeletal dynamics due to a more ordered lipid organization in the plasma membrane.
Visualization of Active Glucocerebrosidase in Rodent Brain with High Spatial Resolution following In Situ Labeling with Fluorescent Activity Based Probes.
Aerts et al., Amsterdam, Netherlands. In Plos One, 2014
In cells, glucosylceramide is also degraded outside lysosomes by the enzyme glucosylceramidase 2 (GBA2) of which inherited deficiency is associated with ataxias.
Reducing GBA2 Activity Ameliorates Neuropathology in Niemann-Pick Type C Mice.
Aerts et al., Amsterdam, Netherlands. In Plos One, 2014
Besides lysosomal GBA, cells also contain a non-lysosomal glucosylceramidase (GBA2).
Genetics of dizziness: cerebellar and vestibular disorders.
Lopez-Escamez et al., Almería, Spain. In Curr Opin Neurol, 2014
RECENT FINDINGS: Whole-exome and targeted sequencing have defined the genetic basis of dizziness including new genes causing ataxia: GBA2, TGM6, ANO10 and SYT14.
[Molecular genetic mechanisms of teratozoospermia].
Wang et al., Changchun, China. In Zhonghua Nan Ke Xue, 2013
Aiming to provide some evidence for the pathogenesis of teratozoospermia, this paper reviews the relevant literature in the past five years addressing such special teratozoospermia as globozoospermia, nuclear vacuoles, decapitated spermatozoa, excessive residual cytoplasm, dysplasia of the fibrous sheath, and primary ciliary dyskinesia, and elaborates on the molecular genetic mechanisms of DPY19L2, AR, PRM1, GBA2, PCI, CREM, TH2A, TH2B, ODF1, Cntrob, OAZ-t, HOOK1, SPEM1, GAT1, PRSS21, 15-LOX, Sptrx, AKAP3, AKAP4, DNAI1, DNAH5, RSPH4A, TXNDC3, CCDC39, LRRC6, LRRC50, KTU and so on.
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.
Yildiz et al., Tübingen, Germany. In Biochem Biophys Res Commun, 2012
GBA1 and GBA2 activities had characteristic differences between the studied fibroblast, liver and brain samples.
Homozygosity for the MTX1 c.184T>A (p.S63T) alteration modifies the age of onset in GBA-associated Parkinson's disease.
Orr-Urtreger et al., Tel Aviv-Yafo, Israel. In Neurogenetics, 2011
Results describe the association between the MTX1 and beta-glucocerebrosidase genes and its possible effect on Parkinson disease.
Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-beta-glucosidase mutant that causes Gaucher disease.
Futerman et al., München, Germany. In Protein Eng Des Sel, 2011
The structure of the N370S acid-beta-glucosidase mutant that causes Gaucher disease was studied.
A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2.
Moracci et al., Napoli, Italy. In J Biol Chem, 2010
Beta-glycosidase from Sulfolobus solfataricus shows distant similarity to the non-lysosomal bile acid beta-glucosidase GBA2 in humans.
Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase.
Schwake et al., Kiel, Germany. In Hum Mol Genet, 2010
Action Myoclonus-Renal Failure Syndrome-causing mutations within LIMP-2 affect the binding to beta-glucocerebrosidase.
Differential sensitivity of mouse strains to an N-alkylated imino sugar: glycosphingolipid metabolism and acrosome formation.
Platt et al., Oxford, United Kingdom. In Pharmacogenomics, 2008
In all recipient mice, irrespective of reproductive phenotype, NB-DNJ has a similar biochemical effect: inhibition of the glucosylceramidase beta-glucosidase 2 and subsequent elevation of glucosylceramide, a glycosphingolipid.
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