Gangliosides and Cell Surface Ganglioside Metabolic Enzymes in the Nervous System.
Central nervous system
Gangliosides
Glycohydrolases
Glycosphingolipids
Neurodegeneration
Neuronal differentiation
Sphingolipid metabolism
Journal
Advances in neurobiology
ISSN: 2190-5215
Titre abrégé: Adv Neurobiol
Pays: United States
ID NLM: 101571545
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
18
10
2022
pubmed:
19
10
2022
medline:
21
10
2022
Statut:
ppublish
Résumé
Gangliosides are a large group of complex lipids found predominantly in the outer layer of the plasma membrane of cells, particularly abundant in nerve endings. Their half-life in the nervous system is short, and their membrane composition and content are strictly connected to their metabolism. The neobiosynthesis of gangliosides starts in the endoplasmic reticulum and is completed in the Golgi apparatus, whereas catabolism occurs primarily in lysosomes. However, the final content of gangliosides in the plasma membrane is defined by other cellular processes.This chapter will discuss structural changes in the oligosaccharide chains of gangliosides, induced by the activity of plasma membrane-associated glycohydrolases and glycosyltransferases. Some of the plasma membrane enzymes originate from fusion processes between intracellular fractions and the plasma membrane, while, others display a different structure. Several of these plasma membrane enzymes have been characterized and some of them seem to have a specific role in the nervous system.
Identifiants
pubmed: 36255680
doi: 10.1007/978-3-031-12390-0_11
doi:
Substances chimiques
Gangliosides
0
Glycosyltransferases
EC 2.4.-
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
305-332Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Nature Switzerland AG.
Références
Acquotti D, Fronza G, Riboni L, Sonnino S, Tettamanti G. Ganglioside lactones:1H-NMR determination of the inner ester position of GD1b-ganglioside lactone naturally occurring in human brain or produced by chemical synthesis. Glycoconj J. 1987;V4:119–27.
doi: 10.1007/BF01049450
Acquotti D, Cantù L, Ragg E, Sonnino S. Geometrical and conformational properties of ganglioside GalNAc-GD1a, IV4GalNAcIV3Neu5AcII3Neu5AcGgOse4Cer. Eur J Biochem. 1994;225(1):271–88.
pubmed: 7925447
doi: 10.1111/j.1432-1033.1994.00271.x
Akita H, Miyagi T, Hata K, Kagayama M. Immunohistochemical evidence for the existence of rat cytosolic sialidase in rat skeletal muscles. Histochem Cell Biol. 1997;107(6):495–503.
Akiyama H, Kobayashi S, Hirabayashi Y, Murakami-Murofushi K. Cholesterol glucosylation is catalyzed by transglucosylation reaction of β-glucosidase 1. Biochem Biophys Res Commun. 2013;441(4):838–43.
pubmed: 24211208
doi: 10.1016/j.bbrc.2013.10.145
Annunziata I, Sano R, d’Azzo A. Mitochondria-associated ER membranes (MAMs) and lysosomal storage diseases. Cell Death Dis. 2018;9(3):328.
pubmed: 29491402
pmcid: 5832421
doi: 10.1038/s41419-017-0025-4
Arantes RM, Andrews NW. A role for synaptotagmin VII-regulated exocytosis of lysosomes in neurite outgrowth from primary sympathetic neurons. J Neurosci. 2006;26(17):4630–7.
pubmed: 16641243
pmcid: 6674075
doi: 10.1523/JNEUROSCI.0009-06.2006
Aureli M, Masilamani AP, Illuzzi G, Loberto N, Scandroglio F, Prinetti A, et al. Activity of plasma membrane beta-galactosidase and beta-glucosidase. FEBS Lett. 2009;583:2469–73.
pubmed: 19577566
doi: 10.1016/j.febslet.2009.06.048
Aureli M, Gritti A, Bassi R, Loberto N, Ricca A, Chigorno V, et al. Plasma membrane-associated glycohydrolases along differentiation of murine neural stem cells. Neurochem Res. 2011a;37:1344–54.
doi: 10.1007/s11064-012-0719-z
Aureli M, Loberto N, Chigorno V, Prinetti A, Sonnino S. Remodeling of sphingolipids by plasma membrane associated enzymes. Neurochem Res. 2011b;36:1636–44.
pubmed: 21181265
doi: 10.1007/s11064-010-0360-7
Aureli M, Loberto N, Lanteri P, Chigorno V, Prinetti A, Sonnino S. Cell surface sphingolipid glycohydrolases in neuronal differentiation and aging in culture. J Neurochem. 2011c;116:891–9.
pubmed: 21214555
doi: 10.1111/j.1471-4159.2010.07019.x
Aureli M, Bassi R, Loberto N, Regis S, Prinetti A, Chigorno V, et al. Cell surface associated glycohydrolases in normal and Gaucher disease fibroblasts. J Inherit Metab Dis. 2012a;35:1081–91.
pubmed: 22526844
doi: 10.1007/s10545-012-9478-x
Aureli M, Loberto N, Bassi R, Ferraretto A, Perego S, Lanteri P, Chigorno V, Sonnino S, Prinetti A. Plasma membrane-associated glycohydrolases activation by extracellular acidification due to proton exchangers. Neurochem Res. 2012b;37:1296–307.
pubmed: 22359055
doi: 10.1007/s11064-012-0725-1
Baron R, Neff L, Louvard D, Courtoy PJ. Cell-mediated extracellular acidification and bone resorption: evidence for a low pH in resorbing lacunae and localization of a 100-kD lysosomal membrane protein at the osteoclast ruffled border. J Cell Biol. 1985;101(6):2210–22.
pubmed: 3905822
doi: 10.1083/jcb.101.6.2210
Bassi R, Riboni L, Sonnino S, Tettamanti G. Lactonization of GD1b ganglioside under acidic conditions. Carbohydr Res. 1989;193:141–6.
pubmed: 2611779
doi: 10.1016/0008-6215(89)85113-4
Bassi R, Chigorno V, Fiorilli A, Sonnino S, Tettamanti G. Exogenous gangliosides GD1b and GD1b-lactone, stably associated to rat brain P2 subcellular fraction, modulate differently the process of protein phosphorylation. J Neurochem. 1991;57:1207–11.
pubmed: 1895103
doi: 10.1111/j.1471-4159.1991.tb08281.x
Bassi R, Riboni L, Tettamanti G. Cultured cerebellar granule cells, but not astrocytes, produce an ester of ganglioside GD1b, presumably GD1b monolactone, from exogenous GD1b. Biochem J. 1994;302(Pt 3):937–42.
pubmed: 7945223
pmcid: 1137320
doi: 10.1042/bj3020937
Bateman KS, Cherney MM, Mahuran DJ, Tropak M, James MN. Crystal structure of beta-hexosaminidase B in complex with pyrimethamine, a potential pharmacological chaperone. J Med Chem. 2011;54:1421–9.
pubmed: 21265544
pmcid: 3201983
doi: 10.1021/jm101443u
Bearpark TM, Stirling JL. A difference in the specificities of human liver N-acetyl-beta-hexosaminidases A and B detected by their activities towards glycosaminoglycan oligosaccharides. Biochem J. 1978;173:997–1000.
pubmed: 708387
pmcid: 1185871
doi: 10.1042/bj1730997
Blott EJ, Griffiths GM. Secretory lysosomes. Nat Rev Mol Cell Biol. 2002;3(2):122–31.
pubmed: 11836514
doi: 10.1038/nrm732
Bremer EG, Hakomori S. GM3 ganglioside induces hamster fibroblast growth inhibition in chemically-defined medium: ganglioside may regulate growth factor receptor function. Biochem Biophys Res Commun. 1982;106(3):711–8.
pubmed: 6288031
doi: 10.1016/0006-291X(82)91769-7
Brocca P, Sonnino S. Dynamic and spatial organization of surface gangliosides. Trends Glycosci Glycotechnol. 1997;9:433–45.
doi: 10.4052/tigg.9.433
Brown DA, London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem. 2000;275(23):17221–4.
pubmed: 10770957
doi: 10.1074/jbc.R000005200
Chambers R. Microdissection studies: I. The visible structure of cell protoplasm and death changes. Am J Physiol. 1917;43:1–12.
doi: 10.1152/ajplegacy.1917.43.1.1
Chigorno V, Cardace G, Pitto M, Sonnino S, Ghidoni R, Tettamanti G. A radiometric assay for ganglioside sialidase applied to the determination of the enzyme subcellular location in cultured human fibroblasts. Anal Biochem. 1986;153:283–94.
pubmed: 3706712
doi: 10.1016/0003-2697(86)90094-1
Chigorno V, Negroni E, Nicolini M, Sonnino S. Activity of 3-ketosphinganine synthase during differentiation and aging of neuronal cells in culture. J Lipid Res. 1997a;38:1163–9.
pubmed: 9215544
doi: 10.1016/S0022-2275(20)37198-4
Chigorno V, Riva C, Valsecchi M, Nicolini M, Brocca P, Sonnino S. Metabolic processing of gangliosides by human fibroblasts in culture–formation and recycling of separate pools of sphingosine. Eur J Biochem. 1997b;250:661–9.
pubmed: 9461288
doi: 10.1111/j.1432-1033.1997.00661.x
Chigorno V, Giannotta C, Ottico E, Sciannamblo M, Mikulak J, Prinetti A, et al. Sphingolipid uptake by cultured cells: complex aggregates of cell sphingolipids with serum proteins and lipoproteins are rapidly catabolized. J Biol Chem. 2005;280:2668–75.
pubmed: 15548542
doi: 10.1074/jbc.M407749200
Chigorno V, Sciannamblo M, Mikulak J, Prinetti A, Sonnino S. Efflux of sphingolipids metabolically labeled with [1–3H]sphingosine, L-[3–3H]serine and [9,10–3H]palmitic acid from normal cells in culture. Glycoconj J. 2006;23:159–65.
pubmed: 16691499
doi: 10.1007/s10719-006-7921-7
Chiricozzi E, Di Biase E, Maggioni M, Lunghi G, Fazzari M, Pomè DY, Casellato R, Loberto N, Mauri L, Sonnino S. GM1 promotes TrkA-mediated neuroblastoma cell differentiation by occupying a plasma membrane domain different from TrkA. J Neurochem. 2019;149(2):231–41.
pubmed: 30776097
doi: 10.1111/jnc.14685
Chiricozzi E, Lunghi G, Di Biase E, Fazzari M, Sonnino S, Mauri L. GM1 ganglioside is a key factor in maintaining the mammalian neuronal functions avoiding neurodegeneration. Int J Mol Sci. 2020;21(3):868.
pmcid: 7037093
doi: 10.3390/ijms21030868
Chiricozzi E, Aureli M, Mauri L, Di Biase E, Lunghi G, Fazzari M, Valsecchi M, Carsana EV, Loberto N, Prinetti A, Sonnino S. Glycosphingolipids. In: Lauc G, Trbojević-Akmačić I, editors. The role of glycosylation in health and disease, Advances in experimental medicine and biology, vol. 1325. Springer; 2021a. p. 61–102.
doi: 10.1007/978-3-030-70115-4_3
Chiricozzi E, Di Biase E, Lunghi G, Fazzari M, Loberto N, Aureli M, Mauri L, Sonnino S. Turning the spotlight on the oligosaccharide chain of GM1 ganglioside. Glycoconj J. 2021b;38(1):101–17.
pubmed: 33620588
pmcid: 7917043
doi: 10.1007/s10719-021-09974-y
Coates PJ. Markers of senescence? J Pathol. 2002;196:371–3.
pubmed: 11920730
doi: 10.1002/path.1073
Crespo PM, Demichelis VT, Daniotti JL. Neobiosynthesis of glycosphingolipids by plasma membrane-associated glycosyltransferases. J Biol Chem. 2010;285:29179–90.
pubmed: 20639193
pmcid: 2937948
doi: 10.1074/jbc.M110.123422
Da Silva JS, Hasegawa T, Miyagi T, Dotti CG, Abad-Rodriguez J. Asymmetric membrane ganglioside sialidase activity specifies axonal fate. Nat Neurosci. 2005;8:606–15.
pubmed: 15834419
doi: 10.1038/nn1442
Daniels LB, Coyle PJ, Chiao YB, Glew RH, Labow RS. Purification and characterization of a cytosolic broad specificity beta-glucosidase from human liver. J Biol Chem. 1981;256:13004–13.
pubmed: 6796580
doi: 10.1016/S0021-9258(18)42997-3
Del Favero E, Brocca P, Motta S, Rondelli V, Sonnino S, Cantu L. Nanoscale structural response of ganglioside-containing aggregates to the interaction with sialidase. J Neurochem. 2011;116:833–9.
pubmed: 21214561
doi: 10.1111/j.1471-4159.2010.07031.x
Dimri GP, Lee X, Basile G, Acosta M, Scott G, Roskelley C, et al. A biomarker that identifies senescent human cells in culture and in aging skin in vivo. Proc Natl Acad Sci U S A. 1995;92:9363–7.
pubmed: 7568133
pmcid: 40985
doi: 10.1073/pnas.92.20.9363
Durrie R, Rosenberg A. Anabolic sialosylation of gangliosides in situ in rat brain cortical slices. J Lipid Res. 1989;30:1259–66.
pubmed: 2769077
doi: 10.1016/S0022-2275(20)38282-1
Durrie R, Saito M, Rosenberg A. Endogenous glycosphingolipid acceptor specificity of sialosyltransferase systems in intact Golgi membranes, synaptosomes, and synaptic plasma membranes from rat brain. Biochemistry. 1988;27:3759–64.
pubmed: 3408725
doi: 10.1021/bi00410a036
Evans MK, Robbins JH, Ganges MB, Tarone RE, Nairn RS, Bohr VA. Gene-specific DNA repair in xeroderma pigmentosum complementation groups A, C, D, and F. Relation to cellular survival and clinical features. J Biol Chem. 1993;268:4839–47.
pubmed: 8444862
doi: 10.1016/S0021-9258(18)53473-6
Ferreirinha F, Quattrini A, Pirozzi M, Valsecchi V, Dina G, Broccoli V, et al. Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport. J Clin Invest. 2004;113:231–42.
pubmed: 14722615
pmcid: 311437
doi: 10.1172/JCI200420138
Gatta AT, Levine TP. Piecing together the patchwork of contact sites. Trends Cell Biol. 2017;27(3):214–29.
pubmed: 27717534
doi: 10.1016/j.tcb.2016.08.010
Gatti M, Magri S, Di Bella D, Sarto E, Taroni F, Mariotti C, Nanetti L. Spastic paraplegia type 46: novel and recurrent GBA2 gene variants in a compound heterozygous Italian patient with spastic ataxia phenotype. Neurol Sci. 2021;42(11):4741–5.
pubmed: 34251556
doi: 10.1007/s10072-021-05463-0
Geng YQ, Guan JT, Xu XH, Fu YC. Senescence-associated beta-galactosidase activity expression in aging hippocampal neurons. Biochem Biophys Res Commun. 2010;396:866–9.
pubmed: 20457127
doi: 10.1016/j.bbrc.2010.05.011
Gulbins E, Grassme H. Ceramide and cell death receptor clustering. Biochim Biophys Acta. 2002;1585:139–45.
pubmed: 12531547
doi: 10.1016/S1388-1981(02)00334-7
Hammer MB, Eleuch-Fayache G, Schottlaender LV, Nehdi H, Gibbs JR, Arepalli SK, et al. Mutations in NLGase cause autosomal-recessive cerebellar ataxia with spasticity. Am J Hum Genet. 2013;92:245–51.
pubmed: 23332917
pmcid: 3567281
doi: 10.1016/j.ajhg.2012.12.012
Hasegawa T, Yamaguchi K, Wada T, Takeda A, Itoyama Y, Miyagi T. Molecular cloning of mouse ganglioside sialidase and its increased expression in neuro2a cell differentiation. J Biol Chem. 2000;275:14778.
doi: 10.1016/S0021-9258(19)80662-2
Hata K, Wada T, Hasegawa A, Kiso M, Miyagi T. Purification and characterization of a membrane-associated ganglioside sialidase from bovine brain. J Biochem (Tokyo). 1998;123:899–905.
doi: 10.1093/oxfordjournals.jbchem.a022022
Holopainen JM, Angelova MI, Kinnunen PK. Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes. Biophys J. 2000;78:830–8.
pubmed: 10653795
pmcid: 1300685
doi: 10.1016/S0006-3495(00)76640-9
Huang Q, Shur BD, Begovac PC. Overexpressing cell surface beta 1.4-galactosyltransferase in PC12 cells increases neurite outgrowth on laminin. J Cell Sci. 1995;108(Pt 2):839–47.
pubmed: 7539442
doi: 10.1242/jcs.108.2.839
Iwamori M, Iwamori Y. Changes in the glycolipid composition and characteristic activation of GM3 synthase in the thymus of mouse after administration of dexamethasone. Glycoconj J. 2005;22:119–26.
pubmed: 16133832
doi: 10.1007/s10719-005-0363-9
Jou I, Lee JH, Park SY, Yoon HJ, Joe EH, Park EJ. Gangliosides trigger inflammatory responses via TLR4 in brain glia. Am J Pathol. 2006;168(5):1619–30.
pubmed: 16651628
pmcid: 1606595
doi: 10.2353/ajpath.2006.050924
Kakugawa Y, Wada T, Yamaguchi K, Yamanami H, Ouchi K, Sato I, et al. Up-regulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression. Proc Natl Acad Sci U S A. 2002;99:10718–23.
pubmed: 12149448
pmcid: 125023
doi: 10.1073/pnas.152597199
Kalka D, von Reitzenstein C, Kopitz J, Cantz M. The plasma membrane ganglioside sialidase cofractionates with markers of lipid rafts. Biochem Biophys Res Commun. 2001;283:989–93.
pubmed: 11350083
doi: 10.1006/bbrc.2001.4864
Kamerling JP, Vliegenthart JF. Identification of O-cetylated N-acylneuraminic acids by mass spectrometry. Carbohydr Res. 1975;41:7–17.
pubmed: 1137847
doi: 10.1016/S0008-6215(00)87002-0
Kappagantula S, Andrews MR, Cheah M, Abad-Rodriguez J, Dotti CG, Fawcett JW. Neu3 sialidase-mediated ganglioside conversion is necessary for axon regeneration and is blocked in CNS axons. J Neurosci. 2014;34(7):2477–92.
pubmed: 24523539
pmcid: 6802756
doi: 10.1523/JNEUROSCI.4432-13.2014
Kolter T, Sandhoff K. Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu Rev Cell Dev Biol. 2005;21:81–103.
pubmed: 16212488
doi: 10.1146/annurev.cellbio.21.122303.120013
Kolter T, Sandhoff K. Sphingolipid metabolism diseases. Biochim Biophys Acta. 2006;1758:2057–79.
pubmed: 16854371
doi: 10.1016/j.bbamem.2006.05.027
Kopitz J, von Reitzenstein C, Muhl C, Cantz M. Role of plasma membrane ganglioside sialidase of human neuroblastoma cells in growth control and differentiation. Biochem Biophys Res Commun. 1994;199:1188–93.
pubmed: 8147859
doi: 10.1006/bbrc.1994.1356
Kopitz J, Muhl C, Ehemann V, Lehmann C, Cantz M. Effects of cell surface ganglioside sialidase inhibition on growth control and differentiation of human neuroblastoma cells. Eur J Cell Biol. 1997a;73:1–9.
pubmed: 9174666
Kopitz J, Sinz K, Brossmer R, Cantz M. Partial characterization and enrichment of a membrane-bound sialidase specific for gangliosides from human brain tissue. Eur J Biochem. 1997b;248:527–34.
pubmed: 9346312
doi: 10.1111/j.1432-1033.1997.00527.x
Korschen HG, Yildiz Y, Raju DN, Schonauer S, Bonigk W, Jansen V, et al. The non-lysosomal beta-glucosidase NLGase is a non-integral membrane-associated protein at the endoplasmic reticulum (ER) and Golgi. J Biol Chem. 2012;288:3381–93.
pubmed: 23250757
pmcid: 3561557
doi: 10.1074/jbc.M112.414714
Koynova R, Caffrey M. Phases and phase transitions of the sphingolipids. Biochim Biophys Acta. 1995;1255(3):213–36.
pubmed: 7734437
doi: 10.1016/0005-2760(94)00202-A
Kytzia HJ, Sandhoff K. Evidence for two different active sites on human beta-hexosaminidase A. Interaction of GM2 activator protein with beta-hexosaminidase A. J Biol Chem. 1985;260:7568–72.
pubmed: 3158659
doi: 10.1016/S0021-9258(17)39645-X
Levine T, Loewen C. Inter-organelle membrane contact sites: through a glass, darkly. Curr Opin Cell Biol. 2006;18(4):371–8.
pubmed: 16806880
doi: 10.1016/j.ceb.2006.06.011
Levine TP, Patel S. Signalling at membrane contact sites: two membranes come together to handle second messengers. Curr Opin Cell Biol. 2016;39:77–83.
pubmed: 26922871
doi: 10.1016/j.ceb.2016.02.011
Li RX, Ladisch S. Shedding of human neuroblastoma gangliosides. Biochim Biophys Acta. 1991;1083(1):57–64.
pubmed: 2031938
doi: 10.1016/0005-2760(91)90124-Z
Li YT, Li SC. Enzymatic hydrolysis of glycosphingolipids. Anal Biochem. 1999;273:1–11.
pubmed: 10452793
doi: 10.1006/abio.1999.4191
Liang F, Seyrantepe V, Landry K, Ahmad R, Ahmad A, Stamatos NM, Pshezhetsky AV. Monocyte differentiation up-regulates the expression of the lysosomal sialidase, Neu1, and triggers its targeting to the plasma membrane via major histocompatibility complex class II-positive compartments. J Biol Chem. 2006;281(37):27526–38.
pubmed: 16835219
doi: 10.1074/jbc.M605633200
Lukong KE, Seyrantepe V, Landry K, Trudel S, Ahmad A, Gahl WA, Lefrancois S, Morales CR, Pshezhetsky AV. Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail. J Biol Chem. 2001;276(49):46172–81.
pubmed: 11571282
doi: 10.1074/jbc.M104547200
Lunghi G, Fazzari M, Di Biase E, Mauri L, Sonnino S, Chiricozzi E. The structure of gangliosides hides a code for determining neuronal functions. FEBS Open Bio. 2021;11(12):3193–200.
pubmed: 34003598
pmcid: 8634855
Malekkou A, Samarani M, Drousiotou A, Votsi C, Sonnino S, Pantzaris M, Chiricozzi E, Zamba-Papanicolaou E, Aureli M, Loberto N, Christodoulou K. Biochemical characterization of the GBA2 c.1780G>C missense mutation in lymphoblastoid cells from patients with spastic ataxia. Int J Mol Sci. 2018;19(10):3099.
pmcid: 6213336
doi: 10.3390/ijms19103099
Marques AR, Mirzaian M, Akiyama H, Wisse P, Ferraz MJ, Gaspar P, Ghauharali-van der Vlugt K, Meijer R, Giraldo P, Alfonso P, Irún P, Dahl M, Karlsson S, Pavlova EV, Cox TM, Scheij S, Verhoek M, Ottenhoff R, van Roomen CP, Pannu NS, van Eijk M, Dekker N, Boot RG, Overkleeft HS, Blommaart E, Hirabayashi Y, Aerts JM. Glucosylated cholesterol in mammalian cells and tissues: formation and degradation by multiple cellular β-glucosidases. J Lipid Res. 2016;57(3):451–63.
pubmed: 26724485
pmcid: 4766994
doi: 10.1194/jlr.M064923
Martin E, Schule R, Smets K, Rastetter A, Boukhris A, Loureiro JL, et al. Loss of function of glucocerebrosidase NLGase is responsible for motor neuron defects in hereditary spastic paraplegia. Am J Hum Genet. 2013;92:238–44.
pubmed: 23332916
pmcid: 3567271
doi: 10.1016/j.ajhg.2012.11.021
Masserini M, Sonnino S, Ghidoni R, Chigorno V, Tettamanti G. Galactose oxidase action on GM1 ganglioside in micellar and vesicular dispersions. Biochim Biophys Acta. 1982;688(2):333–40.
pubmed: 7104327
doi: 10.1016/0005-2736(82)90344-3
Matern H, Boermans H, Lottspeich F, Matern S. Molecular cloning and expression of human bile acid beta-glucosidase. J Biol Chem. 2001;276:37929–33.
pubmed: 11489889
doi: 10.1074/jbc.M104290200
Matsui Y, Lombard D, Massarelli R, Mandel P, Dreyfus H. Surface glycosyltransferase activities during development of neuronal cell cultures. J Neurochem. 1986;46:144–50.
pubmed: 3940275
doi: 10.1111/j.1471-4159.1986.tb12937.x
Mazzulli JR, Xu YH, Sun Y, Knight AL, McLean PJ, Caldwell GA, et al. Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell. 2011;146:37–52.
pubmed: 21700325
pmcid: 3132082
doi: 10.1016/j.cell.2011.06.001
Mencarelli S, Cavalieri C, Magini A, Tancini B, Basso L, Lemansky P, et al. Identification of plasma membrane associated mature beta-hexosaminidase A, active towards GM2 ganglioside, in human fibroblasts. FEBS Lett. 2005;579:5501–6.
pubmed: 16212960
doi: 10.1016/j.febslet.2005.08.081
Miyagi T, Sagawa J, Konno K, Handa S, Tsuiki S. Biochemical and immunological studies on two distinct ganglioside-hydrolyzing sialidases from the particulate fraction of rat brain. J Biochem (Tokyo). 1990a;107:787–93.
doi: 10.1093/oxfordjournals.jbchem.a123126
Miyagi T, Sagawa J, Konno K, Tsuiki S. Immunological discrimination of intralysosomal, cytosolic, and two membrane sialidases present in rat tissues. J Biochem (Tokyo). 1990b;107:794–8.
doi: 10.1093/oxfordjournals.jbchem.a123127
Miyagi T, Wada T, Iwamatsu A, Hata K, Yoshikawa Y, Tokuyama S, et al. Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides. J Biol Chem. 1999;274:5004–11.
pubmed: 9988745
doi: 10.1074/jbc.274.8.5004
Miyagi T, Wada T, Yamaguchi K. Roles of plasma membrane-associated sialidase NEU3 in human cancers. Biochim Biophys Acta. 2008a;1780:532–7.
pubmed: 18023981
doi: 10.1016/j.bbagen.2007.09.016
Miyagi T, Wada T, Yamaguchi K, Shiozaki K, Sato I, Kakugawa Y, et al. Human sialidase as a cancer marker. Proteomics. 2008b;8:3303–11.
pubmed: 18651674
doi: 10.1002/pmic.200800248
Miyagi T, Takahashi K, Yamamoto K, Shiozaki K, Yamaguchi K. Biological and pathological roles of ganglioside sialidases. Prog Mol Biol Transl Sci. 2018;156:121–50.
pubmed: 29747812
doi: 10.1016/bs.pmbts.2017.12.005
Monti E, Preti A, Venerando B, Borsani G. Recent development in mammalian sialidase molecular biology. Neurochem Res. 2002;27:649–63.
pubmed: 12374200
doi: 10.1023/A:1020276000901
Nath S, Mandal C, Chatterjee U, Mandal C. Association of cytosolic sialidase Neu2 with plasma membrane enhances Fas-mediated apoptosis by impairing PI3K-Akt/mTOR-mediated pathway in pancreatic cancer cells. Cell Death Dis. 2018;9(2):210.
pubmed: 29434218
pmcid: 5833727
doi: 10.1038/s41419-017-0191-4
Neufeld EB, Cooney AM, Pitha J, Dawidowicz EA, Dwyer NK, Pentchev PG, et al. Intracellular trafficking of cholesterol monitored with a cyclodextrin. J Biol Chem. 1996;271:21604–13.
pubmed: 8702948
doi: 10.1074/jbc.271.35.21604
Oehler C, Kopitz J, Cantz M. Substrate specificity and inhibitor studies of a membrane-bound ganglioside sialidase isolated from human brain tissue. Biol Chem. 2002;383:1735–42.
pubmed: 12530538
doi: 10.1515/BC.2002.194
Olayioye MA, Hausser A. Integration of non-vesicular and vesicular transport processes at the Golgi complex by the PKD-CERT network. Biochim Biophys Acta. 2012;1821:1096–103.
pubmed: 22226883
doi: 10.1016/j.bbalip.2011.12.005
Papini N, Anastasia L, Tringali C, Croci G, Bresciani R, Yamaguchi K, et al. The plasma membrane-associated sialidase MmNEU3 modifies the ganglioside pattern of adjacent cells supporting its involvement in cell-to-cell interactions. J Biol Chem. 2004;279:16989–95.
pubmed: 14970224
doi: 10.1074/jbc.M400881200
Preti A, Fiorilli A, Lombardo A, Caimi L, Tettamanti G. Occurrence of sialyltransferase activity in the synaptosomal membranes prepared from calf brain cortex. J Neurochem. 1980;35:281–96.
pubmed: 6161218
doi: 10.1111/j.1471-4159.1980.tb06263.x
Prinetti A, Chigorno V, Tettamanti G, Sonnino S. Sphingolipid-enriched membrane domains from rat cerebellar granule cells differentiated in culture. A compositional study. J Biol Chem. 2000a;275:11658–65.
pubmed: 10766784
doi: 10.1074/jbc.275.16.11658
Prinetti A, Marano N, Prioni S, Chigorno V, Mauri L, Casellato R, et al. Association of Src-family protein tyrosine kinases with sphingolipids in rat cerebellar granule cells differentiated in culture. Glycoconj J. 2000b;17:223–32.
pubmed: 11201794
doi: 10.1023/A:1026545424720
Prinetti A, Chigorno V, Prioni S, Loberto N, Marano N, Tettamanti G, et al. Changes in the lipid turnover, composition, and organization, as sphingolipid-enriched membrane domains, in rat cerebellar granule cells developing in vitro. J Biol Chem. 2001;276:21136–45.
pubmed: 11264283
doi: 10.1074/jbc.M010666200
Prinz WA. Bridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics. J Cell Biol. 2014;205(6):759–69.
pubmed: 24958771
pmcid: 4068136
doi: 10.1083/jcb.201401126
Proshin S, Yamaguchi K, Wada T, Miyagi T. Modulation of neuritogenesis by ganglioside-specific sialidase (Neu 3) in human neuroblastoma NB-1 cells. Neurochem Res. 2002;27:841–6.
pubmed: 12374221
doi: 10.1023/A:1020269326825
Raiborg C, Wenzel EM, Pedersen NM, Olsvik H, Schink KO, Schultz SW, Vietri M, Nisi V, Bucci C, Brech A, Johansen T, Stenmark H. Repeated ER-endosome contacts promote endosome translocation and neurite outgrowth. Nature. 2015;520(7546):234–8.
pubmed: 25855459
doi: 10.1038/nature14359
Rao SK, Huynh C, Proux-Gillardeaux V, Galli T, Andrews NW. Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis. J Biol Chem. 2004;279(19):20471–9.
pubmed: 14993220
doi: 10.1074/jbc.M400798200
Reddy A, Caler EV, Andrews NW. Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes. Cell. 2001;106:157–69.
pubmed: 11511344
doi: 10.1016/S0092-8674(01)00421-4
Riboni L, Sonnino S, Acquotti D, Malesci A, Ghidoni R, Egge H, et al. Natural occurrence of ganglioside lactones. Isolation and characterization of GD1b inner ester from adult human brain. J Biol Chem. 1986;261:8514–9.
pubmed: 3722160
doi: 10.1016/S0021-9258(19)83940-6
Riboni L, Prinetti A, Bassi R, Tettamanti G. Cerebellar granule cells in culture exhibit a ganglioside-sialidase presumably linked to the plasma membrane. FEBS Lett. 1991;287:42–6.
pubmed: 1879535
doi: 10.1016/0014-5793(91)80012-R
Riboni L, Viani P, Bassi R, Prinetti A, Tettamanti G. The role of sphingolipids in the process of signal transduction. Prog Lipid Res. 1997;36(2–3):153–95.
pubmed: 9624426
doi: 10.1016/S0163-7827(97)00008-8
Rodriguez JA, Piddini E, Hasegawa T, Miyagi T, Dotti CG. Plasma membrane ganglioside sialidase regulates axonal growth and regeneration in hippocampal neurons in culture. J Neurosci. 2001;21:8387–95.
pubmed: 11606627
pmcid: 6762798
doi: 10.1523/JNEUROSCI.21-21-08387.2001
Rothman JE. Mechanisms of intracellular protein transport. Nature. 1994;372(6501):55–63.
pubmed: 7969419
doi: 10.1038/372055a0
Samarani M, Loberto N, Soldà G, Straniero L, Asselta R, Duga S, Lunghi G, Zucca FA, Mauri L, Ciampa MG, Schiumarini D, Bassi R, Giussani P, Chiricozzi E, Prinetti A, Aureli M, Sonnino S. A lysosome-plasma membrane-sphingolipid axis linking lysosomal storage to cell growth arrest. FASEB J. 2018;32(10):5685–702.
pubmed: 29746165
pmcid: 6133699
doi: 10.1096/fj.201701512RR
Saqr HE, Pearl DK, Yates AJ. A review and predictive models of ganglioside uptake by biological membranes. J Neurochem. 1993;61:395–411.
pubmed: 8336130
doi: 10.1111/j.1471-4159.1993.tb02140.x
Schengrund CL, Repman MA. Density-dependent changes in gangliosides and sialidase activity of murine neuroblastoma cells. J Neurochem. 1982;39:940–7.
pubmed: 7119793
doi: 10.1111/j.1471-4159.1982.tb11480.x
Schengrund CL, Rosenberg A. Intracellular location and properties of bovine brain sialidase. J Biol Chem. 1970;245:6196–200.
pubmed: 5484473
doi: 10.1016/S0021-9258(18)62678-X
Schengrund CL, Rosenberg A, Repman MA. Ecto-ganglioside-sialidase activity of herpes simplex virus-transformed hamster embryo fibroblasts. J Cell Biol. 1976;70:555–61.
pubmed: 182699
doi: 10.1083/jcb.70.3.555
Schneider-Jakob HR, Cantz M. Lysosomal and plasma membrane ganglioside GM3 sialidases of cultured human fibroblasts. Differentiation by detergents and inhibitors. Biol Chem Hoppe Seyler. 1991;372:443–50.
pubmed: 1910582
doi: 10.1515/bchm3.1991.372.1.443
Severino J, Allen RG, Balin S, Balin A, Cristofalo VJ. Is beta-galactosidase staining a marker of senescence in vitro and in vivo? Exp Cell Res. 2000;257:162–71.
pubmed: 10854064
doi: 10.1006/excr.2000.4875
Sidransky E, Nalls MA, Aasly JO, Aharon-Peretz J, Annesi G, Barbosa ER, et al. Multicenter analysis of glucocerebrosidase mutations in Parkinson’s disease. N Engl J Med. 2009;361:1651–61.
pubmed: 19846850
pmcid: 2856322
doi: 10.1056/NEJMoa0901281
Simons K, Toomre D. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol. 2000;1(1):31–9.
pubmed: 11413487
doi: 10.1038/35036052
Soderblom C, Stadler J, Jupille H, Blackstone C, Shupliakov O, Hanna MC. Targeted disruption of the Mast syndrome gene SPG21 in mice impairs hind limb function and alters axon branching in cultured cortical neurons. Neurogenetics. 2010;11:369–78.
pubmed: 20661613
pmcid: 5667354
doi: 10.1007/s10048-010-0252-7
Sonnino S, Ghidoni R, Chigorno V, Masserini M, Tettamanti G. Recognition by two-dimensional thin-layer chromatography and densitometric quantification of alkali-labile gangliosides from the brain of different animals. Anal Biochem. 1983;128:104–14.
pubmed: 6846788
doi: 10.1016/0003-2697(83)90350-0
Sonnino S, Chigorno V, Valsecchi M, Bassi R, Acquotti D, Cantu L, et al. Relationship between the regulation of membrane enzyme activities by gangliosides and a possible ganglioside segregation in membrane microdomains. Indian J Biochem Biophys. 1990;27:353–8.
pubmed: 2102479
Sonnino S, Cantu L, Corti M, Acquotti D, Venerando B. Aggregative properties of gangliosides in solution. Chem Phys Lipids. 1994;71:21–45.
pubmed: 8039256
doi: 10.1016/0009-3084(94)02304-2
Sonnino S, Prinetti A, Mauri L, Chigorno V, Tettamanti G. Dynamic and structural properties of sphingolipids as driving forces for the formation of membrane domains. Chem Rev. 2006;106:2111–25.
pubmed: 16771445
doi: 10.1021/cr0100446
Svennerholm L, Månsson JE, Li YT. Isolation and structural determination of a novel ganglioside, a disialosylpentahexosylceramide from human brain. J Biol Chem. 1973;248(2):740–2.
pubmed: 4684701
doi: 10.1016/S0021-9258(19)44435-9
Tettamanti G, Morgan IG, Gombos G, Vincendon G, Mandel P. Sub-synaptosomal localization of brain particulate neuraminidose. Brain Res. 1972;47:515–8.
pubmed: 4642578
doi: 10.1016/0006-8993(72)90661-0
Tettamanti G, Preti A, Lombardo A, Bonali F, Zambotti V. Parallelism of subcellular location of major particulate neuraminidase and gangliosides in rabbit brain cortex. Biochim Biophys Acta. 1973;306:466–77.
pubmed: 4726869
doi: 10.1016/0005-2760(73)90185-9
Tettamanti G, Preti A, Lombardo A, Suman T, Zambotti V. Membrane-bound neuraminidase in the brain of different animals: behaviour of the enzyme on endogenous sialo derivatives and rationale for its assay. J Neurochem. 1975;25:451–6.
pubmed: 1151380
doi: 10.1111/j.1471-4159.1975.tb04349.x
Triggs-Raine B, Mahuran DJ, Gravel RA. Naturally occurring mutations in GM2 gangliosidosis: a compendium. Adv Genet. 2001;44:199–224.
pubmed: 11596984
doi: 10.1016/S0065-2660(01)44081-8
Tringali C, Papini N, Fusi P, Croci G, Borsani G, Preti A, Tortora P, Tettamanti G, Venerando B, Monti E. Properties of recombinant human cytosolic sialidase HsNEU2. The enzyme hydrolyzes monomerically dispersed GM1 ganglioside molecules. J Biol Chem. 2004;279:3169–79.
pubmed: 14613940
doi: 10.1074/jbc.M308381200
Tringali C, Anastasia L, Papini N, Bianchi A, Ronzoni L, Cappellini MD, et al. Modification of sialidase levels and sialoglycoconjugate pattern during erythroid and erytroleukemic cell differentiation. Glycoconj J. 2007a;24:67–79.
pubmed: 17139558
doi: 10.1007/s10719-006-9013-0
Tringali C, Lupo B, Anastasia L, Papini N, Monti E, Bresciani R, et al. Expression of sialidase Neu2 in leukemic K562 cells induces apoptosis by impairing Bcr-Abl/Src kinases signaling. J Biol Chem. 2007b;282:14364–72.
pubmed: 17374613
doi: 10.1074/jbc.M700406200
Ueno S, Saito S, Wada T, Yamaguchi K, Satoh M, Arai Y, et al. Plasma membrane-associated sialidase is up-regulated in renal cell carcinoma and promotes interleukin-6-induced apoptosis suppression and cell motility. J Biol Chem. 2006;281:7756–64.
pubmed: 16428383
doi: 10.1074/jbc.M509668200
Valaperta R, Chigorno V, Basso L, Prinetti A, Bresciani R, Preti A, et al. Plasma membrane production of ceramide from ganglioside GM3 in human fibroblasts. FASEB J. 2006;20:1227–9.
pubmed: 16645048
doi: 10.1096/fj.05-5077fje
Valaperta R, Valsecchi M, Rocchetta F, Aureli M, Prioni S, Prinetti A, et al. Induction of axonal differentiation by silencing plasma membrane-associated sialidase Neu3 in neuroblastoma cells. J Neurochem. 2007;100:708–19.
pubmed: 17176265
doi: 10.1111/j.1471-4159.2006.04279.x
Valsecchi M, Palestini P, Chigorno V, Sonnino S, Tettamanti G. Changes in the ganglioside long-chain base composition of rat cerebellar granule cells during differentiation and aging in culture. J Neurochem. 1993;60(1):193–6.
pubmed: 8417139
doi: 10.1111/j.1471-4159.1993.tb05837.x
Valsecchi M, Palestini P, Chigorno V, Sonnino S. Age-related changes of the ganglioside long-chain base composition in rat cerebellum. Neurochem Int. 1996;28:183–7.
pubmed: 8719707
doi: 10.1016/0197-0186(95)00069-0
Van Weely S, Brandsma M, Strijland A, Tager JM, Aerts JM. Demonstration of the existence of a second, non-lysosomal glucocerebrosidase that is not deficient in Gaucher disease. Biochim Biophys Acta. 1993;1181:55–62.
pubmed: 8457606
doi: 10.1016/0925-4439(93)90090-N
Veldman RJ, Klappe K, Hinrichs J, Hummel I, van der Schaaf G, Sietsma H, et al. Altered sphingolipid metabolism in multidrug-resistant ovarian cancer cells is due to uncoupling of glycolipid biosynthesis in the Golgi apparatus. FASEB J. 2002;16:1111–3.
pubmed: 12039850
doi: 10.1096/fj.01-0863fje
Venable ME, Lee JY, Smyth MJ, Bielawska A, Obeid LM. Role of ceramide in cellular senescence. J Biol Chem. 1995;270:30701–8.
pubmed: 8530509
doi: 10.1074/jbc.270.51.30701
Venerando B, Cestaro B, Fiorilli A, Ghidoni R, Preti A, Tettamanti G. Kinetics of Vibrio cholerae sialidase action on gangliosidic substrates at different supramolecular-organizational levels. Biochem J. 1982;203(3):735–42.
pubmed: 7115311
pmcid: 1158290
doi: 10.1042/bj2030735
Venerando B, Fiorilli A, Croci G, Tringali C, Goi G, Mazzanti L, et al. Acidic and neutral sialidase in the erythrocyte membrane of type 2 diabetic patients. Blood. 2002;99:1064–70.
pubmed: 11807014
doi: 10.1182/blood.V99.3.1064
Vilcaes AA, Demichelis VT, Daniotti JL. Trans-activity of plasma membrane-associated ganglioside sialyltransferase in mammalian cells. J Biol Chem. 2011;286(36):31437–46. https://doi.org/10.1074/jbc.M111.257196 .
doi: 10.1074/jbc.M111.257196
pubmed: 21768099
pmcid: 3173134
Vinogradova MV, Michaud L, Mezentsev AV, Lukong KE, El-Alfy M, Morales CR, Potier M, Pshezhetsky AV. Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation. Biochem J. 1998;330(Pt 2):641–50.
pubmed: 9480870
pmcid: 1219185
doi: 10.1042/bj3300641
Von Reitzenstein C, Kopitz J, Schuhmann V, Cantz M. Differential functional relevance of a plasma membrane ganglioside sialidase in cholinergic and adrenergic neuroblastoma cell lines. Eur J Biochem. 2001;268:326–33.
doi: 10.1046/j.1432-1033.2001.01883.x
Wada T, Yoshikawa Y, Tokuyama S, Kuwabara M, Akita H, Miyagi T. Cloning, expression, and chromosomal mapping of a human ganglioside sialidase. Biochem Biophys Res Commun. 1999;261:21–7.
pubmed: 10405317
doi: 10.1006/bbrc.1999.0973
Wallom KL, Fernández-Suárez ME, Priestman DA, et al. Glycosphingolipid metabolism and its role in ageing and Parkinson’s disease. Glycoconj J. 2022;39(1):39–53.
pubmed: 34757540
doi: 10.1007/s10719-021-10023-x
Wang J, Wu G, Miyagi T, Lu ZH, Ledeen RW. Sialidase occurs in both membranes of the nuclear envelope and hydrolyzes endogenous GD1a. J Neurochem. 2009;111(2):547–54.
pubmed: 19686243
doi: 10.1111/j.1471-4159.2009.06339.x
Xu YH, Barnes S, Sun Y, Grabowski GA. Multi-system disorders of glycosphingolipid and ganglioside metabolism. J Lipid Res. 2010;51:1643–75.
pubmed: 20211931
pmcid: 2882741
doi: 10.1194/jlr.R003996
Yildiz Y, Matern H, Thompson B, Allegood JC, Warren RL, Ramirez DM, et al. Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility. J Clin Invest. 2006;116:2985–94.
pubmed: 17080196
pmcid: 1626112
doi: 10.1172/JCI29224
Yu RK. Development regulation of ganglioside metabolism. Prog Brain Res. 1994;101:31–44.
pubmed: 8029460
doi: 10.1016/S0079-6123(08)61938-X
Yu RK, Bieberich E, Xia T, Zeng G. Regulation of ganglioside biosynthesis in the nervous system. J Lipid Res. 2004;45:783–93.
pubmed: 15087476
doi: 10.1194/jlr.R300020-JLR200