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Getting rid of intracellular Aβ- loss of cellular degradation leads to transfer between connected neurons
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Avdelningen för cellbiologi. Linköpings universitet, Hälsouniversitetet.
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Avdelningen för inflammationsmedicin. Linköpings universitet, Hälsouniversitetet. Östergötlands Läns Landsting, Diagnostikcentrum, Klinisk patologi och klinisk genetik.
2014 (Engelska)Ingår i: Current pharmaceutical design, ISSN 1381-6128, E-ISSN 1873-4286, Vol. 20, nr 15, s. 2458-2468Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The sporadic, late onset form of Alzheimers disease (AD) shares pathological hallmarks with the familial form; however, no clear reason for increased beta-amyloid (A beta) generation has been found in the former. It has long been speculated that the late onset form of AD is caused by reduced degradation and/or clearance of A beta. Indeed, both intracellular degradation systems, the proteasomal and lysosomal systems, have been shown to be defective in AD. Reduced proteasome activity increases levels of intracellular and secreted A beta. Furthermore, accumulation of improperly degraded A beta in the lysosomes causes lysosomal disruption and cell death. We recently showed that oligomeric A beta can be transmitted from one neuron to another, which causes neurotoxicity. In both the donating and receiving cells, A beta accumulates in the endo-lysosomal compartment. It is possible that ineffective degradation of A beta causes its transfer to neighboring neurons, thereby spreading AD pathology. This review summarizes the data underlying the idea of reduced A beta clearance and subsequent A beta spread in AD, and also suggests new therapeutic methods, which are aimed at targeting the degradation systems and synaptic transfer. By enhancing degradation of intracellular accumulated A beta, it can be possible to remove it and avoid A beta-induced neurodegeneration without disturbing the endogenously important pool of secreted A beta. Additionally, drugs targeted to inhibit the spread of intracellular toxic A beta aggregates may also be useful in stopping the progression of pathology, without affecting the level of A beta that normally occurs in the brain.

Ort, förlag, år, upplaga, sidor
Bentham Science Publishers , 2014. Vol. 20, nr 15, s. 2458-2468
Nyckelord [en]
Alzheimers disease; lysosome; proteasome; beta-amyloid; neuron-to-neuron transfer; degradation
Nationell ämneskategori
Cell- och molekylärbiologi
Identifikatorer
URN: urn:nbn:se:liu:diva-107844DOI: 10.2174/13816128113199990501ISI: 000336169300002PubMedID: 23859554OAI: oai:DiVA.org:liu-107844DiVA, id: diva2:727875
Tillgänglig från: 2014-06-23 Skapad: 2014-06-23 Senast uppdaterad: 2018-01-11Bibliografiskt granskad

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Agholme, LottaHallbeck, Martin

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