Relevant bibliographies by topics / Glucosylceramidase

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Glucosylceramidase'

Author: Grafiati
Published: 4 June 2021
Last updated: 7 July 2024

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Journal articles on the topic "Glucosylceramidase"

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

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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Glucosylceramidase"

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Lecourt, Séverine. "Mécanismes cellulaires et moléculaires régissant la biologie des cellules souches médullaires dans la maladie de Gaucher de type 1." Paris 7, 2011. http://www.theses.fr/2011PA077122.

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La maladie de Gaucher est une maladie génétique rare liée à des mutations dans le gène codant pour la glucocérébrosidase (GBA). Dans la maladie de Gaucher de type 1, l'accumulation de glucosylcéramide dans les lysosomes des cellules affectées provoque des manifestations cliniques hétérogènes incluant des atteintes viscérales, hématologiques et osseuses dont les mécanismes physiopathologiques sont encore mal connus à ce jour. L'objectif de ce travail de thèse a été d'étudier la biologie fonctionnelle de populations cellulaires non encore étudiées dans le contexte de cette pathologie, en particu
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Spitz, Mariana. "Mutações da glicocerebrosidade em pacientes com doença de Parkinson." Universidade de São Paulo, 2006. http://www.teses.usp.br/teses/disponiveis/5/5138/tde-05022007-123329/.

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Introdução: A doença de Parkinson é uma enfermidade neurodegenerativa decorrente da perda de neurônios dopaminérgicos na substância negra, principalmente, e em outras regiões cerebrais. Caracteriza-se clinicamente por tremor, rigidez, bradicinesia e instabilidade postural. O tratamento é sintomático e consiste essencialmente na reposição da dopamina deficiente. A etiologia da doença de Parkinson ainda não é conhecida, mas os recentes avanços da Neurologia trouxeram novos conhecimentos acerca dos mecanismos fisiopatológicos envolvidos. Disfunção mitocondrial, estresse oxidativo e degradação de
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Melser, Su. "Implication du Glucosylceramide dans la voie sécretoire des plantes." Thesis, Bordeaux 2, 2009. http://www.theses.fr/2009BOR21637/document.

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Le rôle des lipides comme des acteurs moléculaires de la voie sécrétoire des plantes n'est pas encore complètement élucidé. Le Glucosylceramide (GlcCer) est synthétisé par la Glucosylceramide synthase (GCS) chez les plantes et constitue un des sphingolipides complexes clé dans les membranes, mais on connaît peu les exigences cellulaires pour le GlcCer. Cette étude repose sur le blocage de la biosynthèse de GlcCer, par l'utilisation d'inhibiteurs chez le tabac et l’arabidopsis, et la production de mutants d'Arabidopsis, pour déterminer l'impact de la biosynthèse du GlcCer sur la dynamique endom
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Dupre, Tess V., Mark A. Doll, Parag P. Shah, et al. "Inhibiting glucosylceramide synthase exacerbates cisplatin-induced acute kidney injury." AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2017. http://hdl.handle.net/10150/624924.

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Acute kidney injury (AKI), resulting from chemotherapeutic agents such as cisplatin, remains an obstacle in the treatment of cancer. Cisplatin-induced AKI involves apoptotic and necrotic cell death, pathways regulated by sphingolipids such as ceramide and glucosylceramide. Results from this study indicate that C57BL/6J mice treated with cisplatin had increased ceramide and hexosylceramide levels in the renal cortex 72 h following cisplatin treatment. Pretreatment of mice with inhibitors of acid sphingomyelinase and de novo ceramide synthesis (amitriptyline and myriocin, respectively) prevented
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Breen, Imogen Zofia. "Glucosylceramide metabolism : from 3D structure to the development of selective chemical probes." Thesis, University of York, 2017. http://etheses.whiterose.ac.uk/19181/.

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Gaucher's disease, the most prevalent of the lysosomal storage disorders, is caused by insufficient lysosomal glucocerebrosidase (GBA1) activity. This is the result of point mutations in the encoding gene, GBA1. The consequence of this reduction in activity is an accumulation of GBA1's substrate, glucosylceramide, in the lysosomes, leading to the various pathologies of Gaucher’s disease. Treatment approaches for Gaucher's disease range include enzyme replacement therapy, substrate reduction therapy and the use of small molecules to stabilise mutant forms of the enzyme – pharmacological chapero
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Raju, Diana Nancy [Verfasser]. "Non-lysosomal accumulation of glucosylceramide alters cytoskeletal dynamics causing globozoospermia / Diana Nancy Raju." Bonn : Universitäts- und Landesbibliothek Bonn, 2015. http://d-nb.info/107728974X/34.

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Bonte, Marie-Amandine. "Impact de l'inhibition de l'activité de la glucocérébrosidase sur les évènements moléculaires associés à la maladie de Parkinson." Electronic Thesis or Diss., Université de Lille (2022-....), 2024. https://pepite-depot.univ-lille.fr/ToutIDP/EDBSL/2024/2024ULILS012.pdf.

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La maladie de Parkinson est une maladie neurodégénérative progressive caractérisée par la perte de neurones dopaminergiques, l’accumulation de lésions intraneuronales nommées corps de Lewy et l’accumulation en fer au niveau de la substance noire. Des mutations touchant le gène GBA, codant pour la glucocérébrosidase lysosomale, ont été associées au risque de survenue de la maladie de Parkinson. La glucocérébrosidase est une enzyme impliquée dans l’hydrolyse des glucosylcéramides en glucose et céramides modifiant ainsi la composition lipidique membranaire. Son activité enzymatique est réduite da
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Amen, Nicole [Verfasser], and Peter [Akademischer Betreuer] Angel. "The role of Glucosylceramides in Keratinocyte Differentiation and Epidermal Barrier Function / Nicole Amen ; Betreuer: Peter Angel." Heidelberg : Universitätsbibliothek Heidelberg, 2013. http://d-nb.info/1177380560/34.

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Singh, Priyanka. "The Role of Neutral Sphingolipids in the Pathogenesis of Parkinson Disease and Dementia with Lewy Bodies." Thèse, Université d'Ottawa / University of Ottawa, 2013. http://hdl.handle.net/10393/24029.

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The molecular mechanisms underlying the association between mutations in GBA1 and risk of developing the ‘synucleinopathy’ disorders Parkinson’s disease (PD) and dementia with Lewy bodies (DLB) remain elusive. To better understand the precise molecular cascade that connects GBA1 mutations with α-synuclein dysregulation, a modified lipid extraction and HPTLC protocol was optimized to detect changes in levels of neutral sphingolipids (SLs) from neural cells and tissue expressing wild-type (WT) GBA1, mutant GBA1, or both. We demonstrate that mutant GBA1 does not confer a dominant-negative effect
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Ito, Mitsuru. "Possible role of ceramide as an indicator of chemoresistance : decrease of the ceramide content via activation of glucosylceramide synthase and sphingomyelin synthase in chemoresistant leukemia." Kyoto University, 2003. http://hdl.handle.net/2433/148774.

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Books on the topic "Glucosylceramidase"

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M, Garber Alan, and United States. Congress. Office of Technology Assessment., eds. Federal and private roles in the development and provision of alglucerase therapy for Gaucher disease. Office of Technology Assessment, 1992.

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Plewe, Michael. Synthese modifizierter Glucosylceramide zur Inhibierung der Galactosyltransferase des Glykosphingolipid-Stoffwechsels. Hartung-Gorre, 1991.

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Hwang, Young-Hwan, and York Pei. Autosomal dominant polycystic kidney disease management. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0309_update_001.

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Management of patients with autosomal dominant polycystic kidney disease (ADPKD) currently comprises non-specific measures including promotion of healthy lifestyle, optimization of blood pressure control, and modification of cardiovascular risk factors. A high water intake of 3–4 L per day in patients with glomerular filtration rate greater than 30 mL/min/1.73 m2 may decrease the risk of kidney stones, but its potential benefit in reducing renal cyst growth is presently unproven. Maintenance of a target blood pressure of 130/80 mmHg is recommended by expert clinical guidelines though this is u
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Book chapters on the topic "Glucosylceramidase"

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Schomburg, Dietmar, and Margit Salzmann. "Glucosylceramidase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_36.

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Timson, David J., Richard J. Reece, James B. Thoden, et al. "Glucosylceramidase Activator Deficiency." In Encyclopedia of Molecular Mechanisms of Disease. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_6768.

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Vaccaro, Anna Maria, Michele Muscillo, Elisabetta Gallozzi, Rosa Salvioli, Massimo Tatti, and Kunihiko Suzuki. "A New Glucosylceramidase Activator in Human Placenta." In Enzymes of Lipid Metabolism II. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5212-9_49.

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Christomanou, Helen, Annemarie Aignesberger, Norbert Herschkowitz, and Ulrich N. Wiesmann. "Etiology of a New Identified Gaucher Disease Variant without Glucosylceramidase Defect." In Lipid Storage Disorders. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1029-7_10.

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Vaccaro, Anna Maria, Michele Muscillo, Rosa Salvioli, Massimo Tatti, and Elisabetta Gallozzi. "The Role of a New Glucosylceramidase Activator Protein in the Binding of the Enzyme to its Natural Substrate." In Lipid Storage Disorders. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1029-7_42.

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Messner, Maria C., and Myles C. Cabot. "Glucosylceramide in Humans." In Advances in Experimental Medicine and Biology. Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6741-1_11.

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Sarmientos, Francesco, Günter Schwarzmann, and Konrad Sandhoff. "Specificity of Human Glucosylceramide ß-Glucosidase Towards Structurally Modified Glucosylceramides in a Liposomal Assay-System." In Enzymes of Lipid Metabolism II. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5212-9_42.

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Shayman, James A. "Glucosylceramide and Galactosylceramide Synthase." In Sphingolipid Biology. Springer Japan, 2006. http://dx.doi.org/10.1007/4-431-34200-1_6.

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Shayman, James A., Vania Hinkovska-Galcheva, and Liming Shu. "Inhibitors of Glucosylceramide Synthase." In Glycolipids. Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-2910-9_20.

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Nakajima, Kazuki, Ayako Kohyama-Koganeya, and Yoshio Hirabayashi. "Profiling of Glucosylceramides by Liquid Chromatography-Tandem Mass Spectrometry." In Glycoscience: Biology and Medicine. Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_123-1.

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Conference papers on the topic "Glucosylceramidase"

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Bhinge, Kaustubh N., Vineet Gupta, and Yong Yu Liu. "Abstract 3441: Silencing glucosylceramide synthase using MBO-asGCS eliminates tumor metastasis." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3441.

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Gupta, Vineet, Kaustubh N. Bhinge, and Yong Yu Liu. "Abstract 4365: Glucosylceramide synthase promotes cancer stem cells accumulating in chemotherapy." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4365.

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van Hell, Albert J., Menno van Lummel, Gerben A. Koning, Wim J. van Blitterswijk, and Marcel Verheij. "Abstract 5527: Short-chain glucosylceramide improves doxorubicin delivery in spontaneous mouse breast carcinomas." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5527.

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Madigan, James P., and Daniel W. Rosenberg. "Abstract 1704: A role for glucosylceramide synthase in resistance to oxaliplatin in colorectal cancer." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-1704.

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Koike, K., E. V. Berdyshev, A. M. Mikosz, et al. "Glucosylceramide Regulates Autophagic Flux and Protects Against Cigarette Smoke Induced Cell Death in Lung Endothelial Cells." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5373.

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Bhinge, Kaustubh N., Vineet Gupta, Sharon Meyer, Benny Blaylock, Qian-Jin Zhang, and Yong Yu Liu. "Abstract 4233A: The opposite effects of doxorubicin on bone marrow cells versus cancer cellsin vivodepend on glucosylceramide synthase." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4233a.

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Sumida, Tomomi, Noriyuki Sueyoshi, and Makoto Ito. "UTILIZATION OF GANGLIOSIDE-DEGRADING PAENIBACILLUS SP. TS12 FOR PRODUCTION OF GLUCOSYLCERAMIDE AND MOLECULAR CLONING OF RELATED NOVEL GANGLIOSIDE-DEGRADING EXOGLYCOSIDASES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.739.

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Juul, N., A. Eklund, Q. Li, et al. "A Functional Metagene Incorporating TTK Protein Kinase, Aurora Kinase B and Glucosylceramide Synthase Predicts Response to Treatment in Primary Breast Cancer." In Abstracts: Thirty-Second Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 10‐13, 2009; San Antonio, TX. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-09-2032.

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van Hell, Albert J., Gerben Koning, Jos Jonkers, and Marcel Verheij. "Abstract 2761: Co-administration of the short-chain sphingolipid N-octanoyl-glucosylceramide improves doxorubicin therapy by enhancing intracellular drug accumulation in vivo." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2761.

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Reports on the topic "Glucosylceramidase"

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Liu, Yong-Yu. Antisense Oligonucleotides to Glucosylceramide Synthase Can Reverse Multidrug Resistance in Breast Cancer. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada407440.

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