ArticleThe Biochemical journal1994
Analysis of glucocerebrosidase activity using N-(1-[14C]hexanoyl)-D-erythroglucosylsphingosine demonstrates a correlation between levels of residual enzyme activity and the type of Gaucher disease.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 63 citations in OpenAlex.
- The modifying effect of mutant LRRK2 on mutant GBA1-associated Parkinson disease.Human molecular genetics · 2025Article
- Functional Analysis of HumanCells · 2024Article
- Efficacy of an AAV vector encoding a thermostable form of glucocerebrosidase in alleviating symptoms in a Gaucher disease mouse model.Gene therapy · 2024Article
- Large-scale proteomics analysis of five brain regions from Parkinson's disease patients with a GBA1 mutation.NPJ Parkinson's disease · 2024Article
- Lipids as Emerging Biomarkers in Neurodegenerative Diseases.International journal of molecular sciences · 2023Review
- Article
- Acid ceramidase inhibition ameliorates α-synuclein accumulation upon loss of GBA1 function.Human molecular genetics · 2018Article
- Identification of a feedback loop involving β-glucosidase 2 and its product sphingosine sheds light on the molecular mechanisms in Gaucher disease.The Journal of biological chemistry · 2017Article
- Neuronal accumulation of glucosylceramide in a mouse model of neuronopathic Gaucher disease leads to neurodegeneration.Human molecular genetics · 2014Article
- My journey into the world of sphingolipids and sphingolipidoses.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012Review
- Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases.The Journal of biological chemistry · 2011Article
- Lysosomal lipid storage diseases.Cold Spring Harbor perspectives in biology · 2011Review
- Laboratory and genetic evaluation of Gaucher disease.Wiener medizinische Wochenschrift (1946) · 2010Review
- A critical role for ceramide synthase 2 in liver homeostasis: I. alterations in lipid metabolic pathways.The Journal of biological chemistry · 2010Article
- X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease.EMBO reports · 2003Article
- Murine MHC class II locus control region drives expression of human beta-glucocerebrosidase in antigen presenting cells of transgenic mice.Gene therapy · 1999Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Glucosylceramide, a degradation product of complex glycosphingolipids, is hydrolysed in lysosomes by glucocerebrosidase (GlcCerase). Mutations in the human GlcCerase gene cause a reduction in GlcCerase activity and accumulation of glucosylceramide, which results in the onset of Gaucher disease, the most common lysosomal storage disease. Significant clinical heterogeneity is observed in Gaucher disease, with three main types known, but no clear correlation has been reported between the different types and levels of residual GlcCerase activity. We now demonstrate that a correlation exists by using a radioactive, short-acyl chain substrate, N-(1-[14C]hexanoyl)-D-erythro-glucosylsphingosine ([14C]hexanoyl-GlcCer). This substrate rapidly transferred into biological membranes in the absence of detergent [Futerman and Pagano (1991) Biochem. J. 280, 295-302] and was hydrolyzed to N-(1-[14C]hexanoyl)-D-erythro-sphingosine ([14C]hexanoyl-Cer) both in vitro and in situ, with an acid pH optimum. A strict correlation was observed between levels of [14C]hexanoyl-GlcCer hydrolysis and Gaucher type in human skin fibroblasts. The mean residual activity measured in vitro for 3 h incubation in type 1 Gaucher fibroblasts (the mild form of the disease) was 46.3 +/- 4.6 nmol of [14C]hexanoyl-Cer formed per mg protein (n = 9), and in type 2 and 3 fibroblasts (the neuronopathic forms of the disease) was 19.6 +/- 6.5 (n = 9). A similar correlation was observed when activity was measured in situ, suggesting that the clinical severity of a lysosomal storage disease is related to levels of residual enzyme activity.
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