Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1 (Articolo in rivista)

Type
Label
  • Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1 (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1096/fj.11-189381 (literal)
Alternative label
  • Bucciantini Monica [ 2,3 ] ; Nosi Daniele [ 4 ] ; Forzan Mario [ 5 ] ; Russo Edda [ 2 ] ; Calamai Martino [ 6 ] ; Pieri Laura [ 1 ] ; Formigli Lucia [ 4 ] ; Quercioli Franco [ 7 ] ; Soria Silvia [ 8 ] ; Pavone Francesco [ 6 ] ; Savistchenko Jimmy [ 1 ] ; Melki Ronald [ 1,5 ] ; Stefani Massimo [ 2,3 ] (2012)
    Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1
    in The FASEB journal
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Bucciantini Monica [ 2,3 ] ; Nosi Daniele [ 4 ] ; Forzan Mario [ 5 ] ; Russo Edda [ 2 ] ; Calamai Martino [ 6 ] ; Pieri Laura [ 1 ] ; Formigli Lucia [ 4 ] ; Quercioli Franco [ 7 ] ; Soria Silvia [ 8 ] ; Pavone Francesco [ 6 ] ; Savistchenko Jimmy [ 1 ] ; Melki Ronald [ 1,5 ] ; Stefani Massimo [ 2,3 ] (literal)
Pagina inizio
  • 818 (literal)
Pagina fine
  • 831 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 26 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • [ 1 ] CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France [ 2 ] Univ Florence, Dept Biochem Sci, Florence, Italy [ 3 ] Univ Florence, Res Ctr Mol Basis Neurodegenerat, Florence, Italy [ 4 ] Univ Florence, Dept Anat Histol & Forens Med, Florence, Italy [ 5 ] Univ Pisa, Dept Anim Pathol Food Prophylaxis & Hyg, Pisa, Italy [ 6 ] Univ Florence, European Lab Nonlinear Spect LENS, Florence, Italy [ 7 ] Consiglio Nazl Ric Florence Res Area, Natl Opt Inst, Florence, Italy [ 8 ] Consiglio Nazl Ric Florence Res Area, Nello Carrara Inst Appl Phys, Florence, Italy (literal)
Titolo
  • Toxic effects of amyloid fibrils on cell membranes: The importance of ganglioside GM1 (literal)
Abstract
  • The interaction of amyloid aggregates with the cell plasma membrane is currently considered among the basic mechanisms of neuronal dysfunction in amyloid neurodegeneration. We used amyloid oligomers and fibrils grown from the yeast prion Sup35p, responsible for the specific prion trait [PSI +], to investigate how membrane lipids modulate fibril interaction with the membranes of cultured H-END cells and cytotoxicity. Sup35p shares no homology with endogenous mammalian polypeptide chains. Thus, the generic toxicity of amyloids and the molecular events underlying cell degeneration can be investigated without interference with analogous polypeptides encoded by the cell genome. Sup35 fibrils bound to the cell membrane without increasing its permeability to Ca 2+. Fibril binding resulted in structural reorganization and aggregation of membrane rafts, with GM1 clustering and alteration of its mobility. Sup35 fibril binding was affected by GM1 or its sialic acid moiety, but not by cholesterol membrane content, with complete inhibition after treatment with fumonisin B1 or neuraminidase. Finally, cell impairment resulted from caspase-8 activation after Fas receptor translocation on fibril binding to the plasmamembrane. Our observations suggest that amyloid fibrils induce abnormal accumulation and overstabilization of raft domains in the cell membrane and provide a reasonable, although not unique, mechanistic and molecular explanation for fibril toxicity (literal)
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