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@ARTICLE{Sandhoff:182155,
      author       = {R. Sandhoff$^*$ and K. Sandhoff},
      title        = {{N}euronal {G}anglioside and {G}lycosphingolipid ({GSL})
                      {M}etabolism and {D}isease : {C}ascades of {S}econdary
                      {M}etabolic {E}rrors {C}an {G}enerate {C}omplex
                      {P}athologies (in {LSD}s).},
      journal      = {Advances in neurobiology},
      volume       = {29},
      issn         = {2190-5215},
      address      = {New York, NY},
      publisher    = {Springer},
      reportid     = {DKFZ-2022-02466},
      isbn         = {978-3-031-12389-4 (print)},
      pages        = {333-390},
      year         = {2023},
      note         = {#EA:A411# / Adv Neurobiol = 2190-5223},
      abstract     = {Glycosphingolipids (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).},
      subtyp        = {Review Article},
      keywords     = {Alzheimer (Other) / Catabolism (Other) / Degradation
                      (Other) / Development (Other) / Endosomal pathway (Other) /
                      Frontal lobe dementia (Other) / Ganglio-series (Other) /
                      Ganglioside (Other) / Genetic disease (Other) / Glycolipid
                      (Other) / Glycosphingolipid (Other) / Glycosyltransferase
                      (Other) / Hydrolase (Other) / Intra-lysosomal luminal
                      vesicle (ILV) (Other) / Lysosomal storage disease (LSD)
                      (Other) / Lysosome (Other) / Membrane-surface (Other) /
                      Metabolism (Other) / Neurodegenerative disease (Other) /
                      Neuron (Other) / Organelle (Other) / Parkinson (Other) /
                      Receptor (Other) / Secondary storage (Other) / Secretory
                      pathway (Other) / Sphingolipid-binding protein (SAP) (Other)
                      / Sphingolipid-transfer protein (Other) / Topology (Other)},
      cin          = {A411},
      ddc          = {570},
      cid          = {I:(DE-He78)A411-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)3 / PUB:(DE-HGF)16},
      pubmed       = {pmid:36255681},
      doi          = {DOI: 10.1007/978-3-031-12390-0_12},
      url          = {https://inrepo02.dkfz.de/record/182155},
}