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Aggregated Aβ1-42 Is Selectively Toxic for Neurons, Whereas Glial Cells Produce Mature Fibrils with Low Toxicity in Drosophila

Artikel i vetenskaplig tidskrift
Författare M. Jonson
S. Nyström
A. Sandberg
M. Carlback
Wojciech Michno
Jörg Hanrieder
A. Starkenberg
K. P. R. Nilsson
S. Thor
P. Hammarström
Publicerad i Cell Chemical Biology
Volym 25
Nummer/häfte 5
Sidor 595-610.e5
ISSN 2451-9456
Publiceringsår 2018
Publicerad vid Institutionen för neurovetenskap och fysiologi, sektionen för psykiatri och neurokemi
Sidor 595-610.e5
Språk en
Länkar dx.doi.org/10.1016/j.chembiol.2018....
Ämnesord Alzheimer's disease, amyloid polymorphism, Aβ1-42, cytotoxicity, Drosophila melanogaster, Gal4/UAS, glial cells, neurodegeneration, neurons, amyloid, amyloid beta protein[1-42], green fluorescent protein, protein aggregate, animal experiment, animal tissue, Article, controlled study, Drosophila, glia cell, locomotion, motoneuron, nonhuman, phenotype, priority journal, protein aggregation, protein conformation, protein expression, retina
Ämneskategorier Neurovetenskaper

Sammanfattning

The basis for selective vulnerability of certain cell types for misfolded proteins (MPs) in neurodegenerative diseases is largely unknown. This knowledge is crucial for understanding disease progression in relation to MPs spreading in the CNS. We assessed this issue in Drosophila by cell-specific expression of human Aβ1-42 associated with Alzheimer's disease. Expression of Aβ1-42 in various neurons resulted in concentration-dependent severe neurodegenerative phenotypes, and intraneuronal ring-tangle-like aggregates with immature fibril properties when analyzed by aggregate-specific ligands. Unexpectedly, expression of Aβ1-42 from a pan-glial driver produced a mild phenotype despite massive brain load of Aβ1-42 aggregates, even higher than in the strongest neuronal driver. Glial cells formed more mature fibrous aggregates, morphologically distinct from aggregates found in neurons, and was mainly extracellular. Our findings implicate that Aβ1-42 cytotoxicity is both cell and aggregate morphotype dependent. Jonson et al. used transgenic Drosophila to understand cell-specific response to protein aggregates in neurodegenerative disease. They demonstrate that the Alzheimer-associated peptide Aβ1-42 form various amyloid structures with different toxic properties when expressed in different cell types of the brain. © 2018 Elsevier Ltd

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