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Journal articles on the topic 'Glucosylceramidase'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 July 2024

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1

Dai, Guang-Yi, Jian Yin, Kai-En Li, et al. "The Arabidopsis AtGCD3 protein is a glucosylceramidase that preferentially hydrolyzes long-acyl-chain glucosylceramides." Journal of Biological Chemistry 295, no. 3 (2019): 717–28. http://dx.doi.org/10.1074/jbc.ra119.011274.

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Cellular membranes contain many lipids, some of which, such as sphingolipids, have important structural and signaling functions. The common sphingolipid glucosylceramide (GlcCer) is present in plants, fungi, and animals. As a major plant sphingolipid, GlcCer is involved in the formation of lipid microdomains, and the regulation of GlcCer is key for acclimation to stress. Although the GlcCer biosynthetic pathway has been elucidated, little is known about GlcCer catabolism, and a plant GlcCer-degrading enzyme (glucosylceramidase (GCD)) has yet to be identified. Here, we identified AtGCD3, one of

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2

Dubot, Patricia, Leonardo Astudillo, Nicole Therville, et al. "Are Glucosylceramide-Related Sphingolipids Involved in the Increased Risk for Cancer in Gaucher Disease Patients? Review and Hypotheses." Cancers 12, no. 2 (2020): 475. http://dx.doi.org/10.3390/cancers12020475.

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The roles of ceramide and its catabolites, i.e., sphingosine and sphingosine 1-phosphate, in the development of malignancies and the response to anticancer regimens have been extensively described. Moreover, an abundant literature points to the effects of glucosylceramide synthase, the mammalian enzyme that converts ceramide to β-glucosylceramide, in protecting tumor cells from chemotherapy. Much less is known about the contribution of β-glucosylceramide and its breakdown products in cancer progression. In this chapter, we first review published and personal clinical observations that report o

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3

&NA;. "Glucosylceramidase." Reactions Weekly &NA;, no. 1205 (2008): 13. http://dx.doi.org/10.2165/00128415-200812050-00038.

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4

Vaccaro, A. M., M. Muscillo, R. Salvioli, M. Tatti, E. Gallozzi, and K. Suzuki. "The binding of glucosylceramidase to glucosylceramide is promoted by its activator protein." FEBS Letters 216, no. 2 (1987): 190–94. http://dx.doi.org/10.1016/0014-5793(87)80687-7.

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5

Malekkou, Anna, Maura Samarani, Anthi Drousiotou, et al. "Biochemical Characterization of the GBA2 c.1780G>C Missense Mutation in Lymphoblastoid Cells from Patients with Spastic Ataxia." International Journal of Molecular Sciences 19, no. 10 (2018): 3099. http://dx.doi.org/10.3390/ijms19103099.

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The GBA2 gene encodes the non-lysosomal glucosylceramidase (NLGase), an enzyme that catalyzes the conversion of glucosylceramide (GlcCer) to ceramide and glucose. Mutations in GBA2 have been associated with the development of neurological disorders such as autosomal recessive cerebellar ataxia, hereditary spastic paraplegia, and Marinesco-Sjogren-Like Syndrome. Our group has previously identified the GBA2 c.1780G>C [p.Asp594His] missense mutation, in a Cypriot consanguineous family with spastic ataxia. In this study, we carried out a biochemical characterization of lymphoblastoid cell lines

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6

Dai, Guang-Yi, Jian Yin, Kai-En Li, et al. "The Arabidopsis AtGCD3 protein is a glucosylceramidase that preferentially hydrolyzes long-acyl-chain glucosylceramides." Journal of Biological Chemistry 295, no. 3 (2020): 717–28. http://dx.doi.org/10.1016/s0021-9258(17)49930-3.

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7

Ghisaidoobe, Amar T., Richard J. B. H. N. van den Berg, Saleem S. Butt, et al. "Identification and Development of Biphenyl Substituted Iminosugars as Improved Dual Glucosylceramide Synthase/Neutral Glucosylceramidase Inhibitors." Journal of Medicinal Chemistry 57, no. 21 (2014): 9096–104. http://dx.doi.org/10.1021/jm501181z.

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8

Jatooratthawichot, Peeranat, Chutima Talabnin, Lukana Ngiwsara, et al. "Effect of Expression of Human Glucosylceramidase 2 Isoforms on Lipid Profiles in COS-7 Cells." Metabolites 10, no. 12 (2020): 488. http://dx.doi.org/10.3390/metabo10120488.

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Glucosylceramide (GlcCer) is a major membrane lipid and the precursor of gangliosides. GlcCer is mainly degraded by two enzymes, lysosomal acid β-glucosidase (GBA) and nonlysosomal β-glucosidase (GBA2), which may have different isoforms because of alternative splicing. To understand which GBA2 isoforms are active and how they affect glycosphingolipid levels in cells, we expressed nine human GBA2 isoforms in COS-7 cells, confirmed their expression by qRT-PCR and Western blotting, and assayed their activity to hydrolyze 4-methylumbelliferyl-β-D-glucopyranoside (4MUG) in cell extracts. Human GBA2

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9

Morimoto, S., Y. Kishimoto, J. Tomich, et al. "Interaction of saposins, acidic lipids, and glucosylceramidase." Journal of Biological Chemistry 265, no. 4 (1990): 1933–37. http://dx.doi.org/10.1016/s0021-9258(19)39921-1.

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10

Nagata, Masahiro, Yoshihiro Izumi, Eri Ishikawa та ін. "Intracellular metabolite β-glucosylceramide is an endogenous Mincle ligand possessing immunostimulatory activity". Proceedings of the National Academy of Sciences 114, № 16 (2017): E3285—E3294. http://dx.doi.org/10.1073/pnas.1618133114.

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Sensing and reacting to tissue damage is a fundamental function of immune systems. Macrophage inducible C-type lectin (Mincle) is an activating C-type lectin receptor that senses damaged cells. Notably, Mincle also recognizes glycolipid ligands on pathogens. To elucidate endogenous glycolipids ligands derived from damaged cells, we fractionated supernatants from damaged cells and identified a lipophilic component that activates reporter cells expressing Mincle. Mass spectrometry and NMR spectroscopy identified the component structure as β-glucosylceramide (GlcCer), which is a ubiquitous intrac

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11

Elleder, M. "Glucosylceramide transfer from lysosomes—the missing link in molecular pathology of glucosylceramidase deficiency: A hypothesis based on existing data." Journal of Inherited Metabolic Disease 29, no. 6 (2006): 707–15. http://dx.doi.org/10.1007/s10545-006-0411-z.

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12

McNeill, Alisdair, Daniel G. Healy, Anthony H. V. Schapira, and Jan-Willem Taanman. "Glucosylceramidase degradation in fibroblasts carrying bi-allelic Parkin mutations." Molecular Genetics and Metabolism 109, no. 4 (2013): 402–3. http://dx.doi.org/10.1016/j.ymgme.2013.06.002.

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13

Karatas, Mesut, Senol Dogan, Emrulla Spahiu, Adna Ašić, Larisa Bešić, and Yusuf Turan. "Enzyme kinetics and inhibition parameters of human leukocyte glucosylceramidase." Heliyon 6, no. 11 (2020): e05191. http://dx.doi.org/10.1016/j.heliyon.2020.e05191.

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14

Vaccaro, Anna Maria, Massimo Tatti, Rosa Salvioli, Fiorella Ciaffoni, and Elisabetta Gallozzi. "Correlation between the activity of glucosylceramidase and its binding to glucosylceramide-containing liposomes. Role of acidic phospholipids and fatty acids." Biochimica et Biophysica Acta (BBA) - General Subjects 1033, no. 1 (1990): 73–79. http://dx.doi.org/10.1016/0304-4165(90)90196-4.

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15

Boot, Rolf G., Marri Verhoek, Wilma Donker-Koopman та ін. "Identification of the Non-lysosomal Glucosylceramidase as β-Glucosidase 2". Journal of Biological Chemistry 282, № 2 (2006): 1305–12. http://dx.doi.org/10.1074/jbc.m610544200.

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16

Vaccaro, Anna Maria, Massimo Tatti, Fiorella Ciaffoni, Rosa Salvioli, and Paola Roncaioli. "Reconstitution of glucosylceramidase on binding to acidic phospholipid-containing vesicles." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1119, no. 3 (1992): 239–46. http://dx.doi.org/10.1016/0167-4838(92)90208-u.

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17

VACCARO, Anna Maria, Michele MUSCILLO, and Kunihiko SUZUKI. "Characterization of human glucosylsphingosine glucosyl hydrolase and comparison with glucosylceramidase." European Journal of Biochemistry 146, no. 2 (1985): 315–21. http://dx.doi.org/10.1111/j.1432-1033.1985.tb08655.x.

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18

BIEBERICH, Erhard, та Günter LEGLER. "Intracellular Activity of Lysosomal Glucosylceramidase Measured with 4-Nonylumbelliferyl β-glucoside". Biological Chemistry Hoppe-Seyler 370, № 2 (1989): 809–18. http://dx.doi.org/10.1515/bchm3.1989.370.2.809.

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19

Vaccaro, Anna Maria, Massimo Tatti, Fiorella Ciaffoni, and Rosa Salvioli. "Factors Affecting the Binding of Glucosylceramidase to Its Natural Substrate Dispersion." Enzyme 42, no. 2 (1989): 87–97. http://dx.doi.org/10.1159/000469014.

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20

Massimo, Aureli, Samarani Maura, Loberto Nicoletta та ін. "Current and Novel Aspects on the Non-lysosomal β-Glucosylceramidase GBA2". Neurochemical Research 41, № 1-2 (2015): 210–20. http://dx.doi.org/10.1007/s11064-015-1763-2.

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21

Overkleeft, Herman S., G. Herma Renkema, Jolanda Neele, et al. "Generation of Specific Deoxynojirimycin-type Inhibitors of the Non-lysosomal Glucosylceramidase." Journal of Biological Chemistry 273, no. 41 (1998): 26522–27. http://dx.doi.org/10.1074/jbc.273.41.26522.

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22

van der Lienden, Martijn J. C., Jan Aten, André R. A. Marques, et al. "GCase and LIMP2 Abnormalities in the Liver of Niemann Pick Type C Mice." International Journal of Molecular Sciences 22, no. 5 (2021): 2532. http://dx.doi.org/10.3390/ijms22052532.

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The lysosomal storage disease Niemann–Pick type C (NPC) is caused by impaired cholesterol efflux from lysosomes, which is accompanied by secondary lysosomal accumulation of sphingomyelin and glucosylceramide (GlcCer). Similar to Gaucher disease (GD), patients deficient in glucocerebrosidase (GCase) degrading GlcCer, NPC patients show an elevated glucosylsphingosine and glucosylated cholesterol. In livers of mice lacking the lysosomal cholesterol efflux transporter NPC1, we investigated the expression of established biomarkers of lipid-laden macrophages of GD patients, their GCase status, and c

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23

Xing You, Hong, Xiaoyang Qi, and Lei Yu. "Real-Time Observation of Phospholipid Bilayer Membrane Restructuring Induced by Protein Molecules using Atomic Force Microscopy." Microscopy and Microanalysis 7, S2 (2001): 858–59. http://dx.doi.org/10.1017/s1431927600030361.

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Atomic force microscopy (AFM) allows the surfaces of native biological materials to be imaged in aqueous solution with submolecular resolution. The ability to perform AFM imaging in aqueous and physiological environment has made it possible to monitor important biological processes in real time at high resolution. Currently, there is a great deal of interest in AFM studies of the structure and property of lipid bilayer membranes and protein interactions with lipid bilayer membranes. Lipid bilayer membranes in biological cells form a permeability barrier, which controls the flow of ions, water,

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24

Oura, Takahiro, and Susumu Kajiwara. "Candida albicans sphingolipid C9-methyltransferase is involved in hyphal elongation." Microbiology 156, no. 4 (2010): 1234–43. http://dx.doi.org/10.1099/mic.0.033985-0.

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C9-methylated glucosylceramide is a fungus-specific sphingolipid. This lipid is a major membrane component in the cell and is thought to play important roles in the growth and virulence of several fungal species. To investigate the importance of the methyl branch of the long-chain base in glucosylceramides in pathogenic fungi, we identified and characterized a sphingolipid C9-methyltransferase gene (MTS1, C9-MethylTransferase for Sphingolipid 1) in the pathogenic yeast Candida albicans. The mts1 disruptant lacked (E,E)-9-methylsphinga-4,8-dienine in its glucosylceramides and contained (E)-sphi

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25

PAAL, Krisztina, Makoto ITO, and Stephen G. WITHERS. "Paenibacillus sp. TS12 glucosylceramidase: kinetic studies of a novel sub-family of family 3 glycosidases and identification of the catalytic residues." Biochemical Journal 378, no. 1 (2004): 141–49. http://dx.doi.org/10.1042/bj20031028.

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GCase (glucosylceramidase) from Paenibacillus sp. TS12, a family 3 glycosidase, hydrolyses the β-glycosidic linkage of glucosylceramide with retention of anomeric configuration via a two-step, double-displacement mechanism. Two carboxyl residues are essential for catalysis, one functioning as a nucleophile and the other as a general acid/base catalyst. p-Nitrophenyl β-d-glucopyranoside [Km=0.27±0.02 mM and kcat/Km=(2.1±0.2)×106 M−1·s−1] and 2,4-dinitrophenyl β-d-glucopyranoside [Km=0.16±0.02 mM and kcat/Km=(2.9±0.4)×106 M−1·s−1] were used for continuous assay of the enzyme. The dependence of k

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26

Yan, Shaomin, and Guang Wu. "Quantitative Relationship Between Mutated Structure of Human Glucosylceramidase and Gaucher Disease Status." International Journal of Peptide Research and Therapeutics 14, no. 3 (2008): 263–71. http://dx.doi.org/10.1007/s10989-008-9142-3.

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27

Vaccaro, Anna Maria, Massimo Tatti, Fiorella Ciaffoni, Rosa Salvioli, Alessandra Barca, and Paola Roncaioli. "Studies on glucosylceramidase binding to phosphatidylserine liposomes: the role of bilayer curvature." Biochimica et Biophysica Acta (BBA) - Biomembranes 1149, no. 1 (1993): 55–62. http://dx.doi.org/10.1016/0005-2736(93)90024-t.

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28

Vaccaro, Anna Maria, Massimo Tatti, Fiorella Ciaffoni, Rosa Salvioli, Bruno Maras, and Alessandra Barca. "Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes." FEBS Letters 336, no. 1 (1993): 159–62. http://dx.doi.org/10.1016/0014-5793(93)81631-9.

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29

Dai, Huanghuang, Akira Otsuka, Kurumi Tanabe, Teruyoshi Yanagita, Jiro Nakayama, and Hiroshi Kitagaki. "Glucosylceramide Changes Bacterial Metabolism and Increases Gram-Positive Bacteria through Tolerance to Secondary Bile Acids In Vitro." International Journal of Molecular Sciences 23, no. 10 (2022): 5300. http://dx.doi.org/10.3390/ijms23105300.

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Glucosylceramide is present in many foods, such as crops and fermented foods. Most glucosylceramides are not degraded or absorbed in the small intestine and pass through the large intestine. Glucosylceramide exerts versatile effects on colon tumorigenesis, skin moisture, cholesterol metabolism and improvement of intestinal microbes in vivo. However, the mechanism of action has not yet been fully elucidated. To gain insight into the effect of glucosylceramide on intestinal microbes, glucosylceramide was anaerobically incubated with the dominant intestinal microbe, Blautia coccoides, and model i

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30

Aureli, Massimo, Maura Samarani, Nicoletta Loberto та ін. "Erratum to: Current and Novel Aspects on the Non-lysosomal β-Glucosylceramidase GBA2". Neurochemical Research 41, № 1-2 (2016): 221. http://dx.doi.org/10.1007/s11064-016-1833-0.

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31

Chludil, Hugo D., Alicia M. Seldes, and Marta S. Maier. "Anasterocerebroside A, a New Glucosylceramide from the Patagonian Starfish Anasterias minuta." Zeitschrift für Naturforschung C 58, no. 5-6 (2003): 433–40. http://dx.doi.org/10.1515/znc-2003-5-624.

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Abstract Eight glucosylceramides (1-8) were isolated from the water-insoluble lipid fraction of a methylene chloride/methanol/water extract of the Patagonian starfish Anasterias minuta. One of the constituents was identified as a new glucosylceramide, anasterocerebroside A (1), while the known glucosylceramide 7 was isolated and characterized for the first time as a pure compound. The structures of 1 and 7 were established by spectroscopic and chemical methods.

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32

Offman, Marc N., Marcin Krol, Israel Silman, Joel L. Sussman, and Anthony H. Futerman. "Molecular Basis of Reduced Glucosylceramidase Activity in the Most Common Gaucher Disease Mutant, N370S." Journal of Biological Chemistry 285, no. 53 (2010): 42105–14. http://dx.doi.org/10.1074/jbc.m110.172098.

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33

Salvioli, Rosa, Massimo Tatti, Fiorella Ciaffoni, and Anna Maria Vaccaro. "Further studies on the reconstitution of glucosylceramidase activity by Sap C and anionic phospholipids." FEBS Letters 472, no. 1 (2000): 17–21. http://dx.doi.org/10.1016/s0014-5793(00)01417-4.

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34

Atsumi, S., C. Nosaka, H. Iinuma, and K. Umezawa. "Accumulation of Tissue Glucosylsphingosine in Gaucher-like Mouse Induced by the Glucosylceramidase Inhibitor Cyclophellitol." Archives of Biochemistry and Biophysics 304, no. 1 (1993): 302–4. http://dx.doi.org/10.1006/abbi.1993.1353.

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35

Dai, Huanghuang, Johan Hariwitonang, Nao Fujiyama, et al. "A Decrease in the Hardness of Feces with Added Glucosylceramide Extracted from Koji In Vitro—A Working Hypothesis of Health Benefits of Dietary Glucosylceramide." Life 14, no. 6 (2024): 739. http://dx.doi.org/10.3390/life14060739.

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Skin barrier function, prevent colon cancer, head and neck cancer, and decrease liver cholesterol. However, the mechanism of action has not yet been elucidated. In this study, we propose a new working hypothesis regarding the health benefits and functions of glucosylceramide: decreased fecal hardness. This hypothesis was verified using an in vitro hardness test. The hardness of feces supplemented with glucosylceramide was significantly lower than that of the control. Based on these results, a new working hypothesis of dietary glucosylceramide was conceived: glucosylceramide passes through the

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36

Pospelova, T. I., and T. N. Babaeva. "RARE BLOOD DISEASES: GAUCHER DISEASE. CASE DESCRIPTION." Sibirskij medicinskij vestnik 7, no. 3 (2023): 42–50. http://dx.doi.org/10.31549/2541-8289-2023-7-3-42-50.

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Gaucher disease is the most common form of hereditary enzymopathies included in the group of lysosomal storage diseases. The disease is based on a hereditary deficiency in the activity of the enzyme glucocerebrosidase (also called glucosylceramidase or acid β-glucosidase) which is involved in the degradation of cellular metabolic products. Gaucher disease is a systemic disease characterized by the same type of clinical manifestations (hepatosplenomegaly, cytopenias, lesions of the skeletal system) but an extremely heterogeneous clinical course. In the article, the authors describe their own cl

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37

Salvioli, Rosa, Susanna Scarpa, Fiorella Ciaffoni, et al. "Glucosylceramidase Mass and Subcellular Localization Are Modulated by Cholesterol in Niemann-Pick Disease Type C." Journal of Biological Chemistry 279, no. 17 (2004): 17674–80. http://dx.doi.org/10.1074/jbc.m313517200.

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38

Tavares, Patricia M., Karin Thevissen, Bruno P. A. Cammue, et al. "In Vitro Activity of the Antifungal Plant Defensin RsAFP2 against Candida Isolates and Its In Vivo Efficacy in Prophylactic Murine Models of Candidiasis." Antimicrobial Agents and Chemotherapy 52, no. 12 (2008): 4522–25. http://dx.doi.org/10.1128/aac.00448-08.

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ABSTRACT We show that RsAFP2, a plant defensin that interacts with fungal glucosylceramides, is active against Candida albicans, inhibits to a lesser extent other Candida species, and is nontoxic to mammalian cells. Moreover, glucosylceramide levels in Candida species correlate with RsAFP2 sensitivity. We found RsAFP2 prophylactically effective against murine candidiasis.

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39

Clark, Laura E., Amanda J. G. Dickinson, and Santiago Lima. "GBA Regulates EMT/MET and Chemoresistance in Squamous Cell Carcinoma Cells by Modulating the Cellular Glycosphingolipid Profile." Cells 12, no. 14 (2023): 1886. http://dx.doi.org/10.3390/cells12141886.

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Glycosphingolipids (GSL) are plasma membrane components that influence molecular processes involved in cancer initiation, progression, and therapeutic responses. They also modulate receptor tyrosine kinases involved in EMT. Therefore, understanding the mechanisms that regulate GSLs in cancer has important therapeutic potential. One critical regulator of GSLs is the lysosomal glucosylceramidase β1 (GBA) that catalyzes the last step in GSL degradation. We show that, in cancer, GBA copy number amplifications and increased expression are widespread. We show that depleting GBA in squamous cell carc

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40

Yildiz, Yildiz, Per Hoffmann, Stefan vom Dahl, et al. "Functional and genetic characterization of the non-lysosomal glucosylceramidase 2 as a modifier for Gaucher disease." Orphanet Journal of Rare Diseases 8, no. 1 (2013): 151. http://dx.doi.org/10.1186/1750-1172-8-151.

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Sansenya, Sompong, Risa Mutoh, Ratana Charoenwattanasatien, Genji Kurisu та James R. Ketudat Cairns. "Expression and crystallization of a bacterial glycoside hydrolase family 116 β-glucosidase fromThermoanaerobacterium xylanolyticum". Acta Crystallographica Section F Structural Biology Communications 71, № 1 (2015): 41–44. http://dx.doi.org/10.1107/s2053230x14025461.

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TheThermoanaerobacterium xylanolyticumgene product TxGH116, a glycoside hydrolase family 116 protein of 806 amino-acid residues sharing 37% amino-acid sequence identity over 783 residues with human glucosylceramidase 2 (GBA2), was expressed inEscherichia coli. Purification by heating, immobilized metal-affinity and size-exclusion chromatography produced >90% pure TxGH116 protein with an apparent molecular mass of 90 kDa on SDS–PAGE. The purified TxGH116 enzyme hydrolyzed thep-nitrophenyl (pNP) glycosidespNP-β-D-glucoside,pNP-β-D-galactoside andpNP-N-acetyl-β-D-glucopyranoside, as well as ce

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42

Woeste, Marina A., Sina Stern, Diana N. Raju, et al. "Species-specific differences in nonlysosomal glucosylceramidase GBA2 function underlie locomotor dysfunction arising from loss-of-function mutations." Journal of Biological Chemistry 294, no. 11 (2019): 3853–71. http://dx.doi.org/10.1074/jbc.ra118.006311.

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43

Aguilera-Herce, Julia, Concepción Panadero-Medianero, María Antonia Sánchez-Romero, Roberto Balbontín, Joaquín Bernal-Bayard, and Francisco Ramos-Morales. "Salmonella Type III Secretion Effector SrfJ: A Glucosylceramidase Affecting the Lipidome and the Transcriptome of Mammalian Host Cells." International Journal of Molecular Sciences 24, no. 9 (2023): 8403. http://dx.doi.org/10.3390/ijms24098403.

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Type III secretion systems are found in many Gram-negative pathogens and symbionts of animals and plants. Salmonella enterica has two type III secretion systems associated with virulence, one involved in the invasion of host cells and another involved in maintaining an appropriate intracellular niche. SrfJ is an effector of the second type III secretion system. In this study, we explored the biochemical function of SrfJ and the consequences for mammalian host cells of the expression of this S. enterica effector. Our experiments suggest that SrfJ is a glucosylceramidase that alters the lipidome

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44

Zhou, Huitong, Yunsheng Zhang, Robert Suter, et al. "A nucleotide substitution in exon 8 of the glucosylceramidase beta gene is associated with Gaucher disease in sheep." Animal Genetics 48, no. 6 (2017): 733–34. http://dx.doi.org/10.1111/age.12613.

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45

Ma, Yubin, Wenxing Ye, Yuchen Cheng, et al. "Metagenomics-Based Analysis of the Effect of Rice Straw Substitution for a Proportion of Whole-Plant Corn Silage on the Rumen Flora Structure and Carbohydrate-Active Enzymes (CAZymes)." Fermentation 9, no. 11 (2023): 954. http://dx.doi.org/10.3390/fermentation9110954.

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The purpose of this study was to investigate the effects of replacing a portion of whole-plant corn silage with straw on the rumen microbial community structure and carbohydrate-active enzyme activity. The experiment employed a single-factor randomized trial design, with eight late-lactation Chinese Holstein dairy cows being randomly divided into two groups of four replicates each. The control group (CS group) was fed a diet consisting of alfalfa silage and a mixture of alfalfa and whole-plant corn silage, while the experimental group (RS group) received a diet in which one-third of the corn s

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46

Du, Sichen, Huayuan Ou, Renjie Cui, et al. "Delivery of Glucosylceramidase Beta Gene Using AAV9 Vector Therapy as a Treatment Strategy in Mouse Models of Gaucher Disease." Human Gene Therapy 30, no. 2 (2019): 155–67. http://dx.doi.org/10.1089/hum.2018.072.

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47

Lahav, Daniël, Bing Liu, Richard J. B. H. N. van den Berg, et al. "A Fluorescence Polarization Activity-Based Protein Profiling Assay in the Discovery of Potent, Selective Inhibitors for Human Nonlysosomal Glucosylceramidase." Journal of the American Chemical Society 139, no. 40 (2017): 14192–97. http://dx.doi.org/10.1021/jacs.7b07352.

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Vaccaro, Anna Maria, Michele Muscillo, Massimo Tatti, Rosa Salvioli, Elisabetta Gallozzi та Kunihiko Suzuki. "Effect of a heat-stable factor in human placenta on glucosylceramidase, glucosylsphingosine glucosyl hydrolase, and acid β-glucosidase activities". Clinical Biochemistry 20, № 6 (1987): 429–33. http://dx.doi.org/10.1016/0009-9120(87)90010-5.

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Salvioli, Rosa, Massimo Tatti, Susanna Scarpa, et al. "The N370S (Asn370→Ser) mutation affects the capacity of glucosylceramidase to interact with anionic phospholipid-containing membranes and saposin C." Biochemical Journal 390, no. 1 (2005): 95–103. http://dx.doi.org/10.1042/bj20050325.

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Abstract:

The properties of the endolysosomal enzyme GCase (glucosylceramidase), carrying the most prevalent mutation observed in Gaucher patients, namely substitution of an asparagine residue with a serine at amino acid position 370 [N370S (Asn370→Ser) GCase], were investigated in the present study. We previously demonstrated that Sap (saposin) C, the physiological GCase activator, promotes the association of GCase with anionic phospholipid-containing membranes, reconstituting in this way the enzyme activity. In the present study, we show that, in the presence of Sap C and membranes containing high lev

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Molina, Yessenia L., David García-Seisdedos, Bohdan Babiy, et al. "Rottlerin Stimulates Exosome/Microvesicle Release Via the Increase of Ceramide Levels Mediated by Ampk in an In Vitro Model of Intracellular Lipid Accumulation." Biomedicines 10, no. 6 (2022): 1316. http://dx.doi.org/10.3390/biomedicines10061316.

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Abstract:

Exosomes/microvesicles originate from multivesicular bodies that allow the secretion of endolysosome components out of the cell. In the present work, we investigated the effects of rottlerin, a polyphenol, on exosome/microvesicle secretion in a model of intracellular lipid trafficking impairment, and elucidated the mechanism of action. In a model of lipid trafficking impairment in C6 glia cells, rottlerin increased ceramide levels, while decreasing hexosylceramide content. This was accompanied by increased exosome/microvesicle secretion, thereby reducing the concentration of lipids in the endo

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