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000182155 020__ $$a978-3-031-12389-4 (print)
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000182155 0247_ $$2doi$$a10.1007/978-3-031-12390-0_12
000182155 0247_ $$2pmid$$apmid:36255681
000182155 0247_ $$2doi$$a DOI: 10.1007/978-3-031-12390-0_12 
000182155 0247_ $$2doi$$aDOI: 10.1007/978-3-031-12390-0_12
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000182155 037__ $$aDKFZ-2022-02466
000182155 041__ $$aEnglish
000182155 082__ $$a570
000182155 1001_ $$0P:(DE-He78)a928ded2085c8911822370cad0b4a728$$aSandhoff, Roger$$b0$$eFirst author$$udkfz
000182155 245__ $$aNeuronal Ganglioside and Glycosphingolipid (GSL) Metabolism and Disease : Cascades of Secondary Metabolic Errors Can Generate Complex Pathologies (in LSDs).
000182155 260__ $$aNew York, NY$$bSpringer$$c2023
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000182155 500__ $$a#EA:A411#  / Adv Neurobiol = 2190-5223
000182155 520__ $$aGlycosphingolipids (GSLs) are a diverse group of membrane components occurring mainly on the surfaces of mammalian cells. They and their metabolites have a role in intercellular communication, serving as versatile biochemical signals (Kaltner et al, Biochem J 476(18):2623-2655, 2019) and in many cellular pathways. Anionic GSLs, the sialic acid containing gangliosides (GGs), are essential constituents of neuronal cell surfaces, whereas anionic sulfatides are key components of myelin and myelin forming oligodendrocytes. The stepwise biosynthetic pathways of GSLs occur at and lead along the membranes of organellar surfaces of the secretory pathway. After formation of the hydrophobic ceramide membrane anchor of GSLs at the ER, membrane-spanning glycosyltransferases (GTs) of the Golgi and Trans-Golgi network generate cell type-specific GSL patterns for cellular surfaces. GSLs of the cellular plasma membrane can reach intra-lysosomal, i.e. luminal, vesicles (ILVs) by endocytic pathways for degradation. Soluble glycoproteins, the glycosidases, lipid binding and transfer proteins and acid ceramidase are needed for the lysosomal catabolism of GSLs at ILV-membrane surfaces. Inherited mutations triggering a functional loss of glycosylated lysosomal hydrolases and lipid binding proteins involved in GSL degradation cause a primary lysosomal accumulation of their non-degradable GSL substrates in lysosomal storage diseases (LSDs). Lipid binding proteins, the SAPs, and the various lipids of the ILV-membranes regulate GSL catabolism, but also primary storage compounds such as sphingomyelin (SM), cholesterol (Chol.), or chondroitin sulfate can effectively inhibit catabolic lysosomal pathways of GSLs. This causes cascades of metabolic errors, accumulating secondary lysosomal GSL- and GG- storage that can trigger a complex pathology (Breiden and Sandhoff, Int J Mol Sci 21(7):2566, 2020).
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000182155 650_7 $$2Other$$aAlzheimer
000182155 650_7 $$2Other$$aCatabolism
000182155 650_7 $$2Other$$aDegradation
000182155 650_7 $$2Other$$aDevelopment
000182155 650_7 $$2Other$$aEndosomal pathway
000182155 650_7 $$2Other$$aFrontal lobe dementia
000182155 650_7 $$2Other$$aGanglio-series
000182155 650_7 $$2Other$$aGanglioside
000182155 650_7 $$2Other$$aGenetic disease
000182155 650_7 $$2Other$$aGlycolipid
000182155 650_7 $$2Other$$aGlycosphingolipid
000182155 650_7 $$2Other$$aGlycosyltransferase
000182155 650_7 $$2Other$$aHydrolase
000182155 650_7 $$2Other$$aIntra-lysosomal luminal vesicle (ILV)
000182155 650_7 $$2Other$$aLysosomal storage disease (LSD)
000182155 650_7 $$2Other$$aLysosome
000182155 650_7 $$2Other$$aMembrane-surface
000182155 650_7 $$2Other$$aMetabolism
000182155 650_7 $$2Other$$aNeurodegenerative disease
000182155 650_7 $$2Other$$aNeuron
000182155 650_7 $$2Other$$aOrganelle
000182155 650_7 $$2Other$$aParkinson
000182155 650_7 $$2Other$$aReceptor
000182155 650_7 $$2Other$$aSecondary storage
000182155 650_7 $$2Other$$aSecretory pathway
000182155 650_7 $$2Other$$aSphingolipid-binding protein (SAP)
000182155 650_7 $$2Other$$aSphingolipid-transfer protein
000182155 650_7 $$2Other$$aTopology
000182155 7001_ $$aSandhoff, Konrad$$b1
000182155 773__ $$0PERI:(DE-600)2590974-5$$aDOI: 10.1007/978-3-031-12390-0_12$$p333-390$$tAdvances in neurobiology$$v29$$x2190-5215$$y2023
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000182155 9141_ $$y2023
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