The dark sides of amyloid in Alzheimer's disease pathogenesis. Issue 5 (31st January 2014)

• Record Type: Journal Article
• Authors: Sorrentino, Pierpaolo; Iuliano, Antonietta; Polverino, Arianna; Jacini, Francesca; Sorrentino, Giuseppe
• Is Part Of: FEBS letters. Volume 588:Issue 5(2014)
• Page Start: 641
• Page End: 652
• Publication Date: 2014-01-31
• Subjects: Aβ -- amyloid β protein -- NFT -- neurofibrillary tangles -- APP -- amyloid precursor protein -- PSs -- presenilins -- NICD -- Notch intracellular domain -- mTOR -- mammalian Target of Rapamycin -- PP2A -- protein phosphatase 2 -- GSK-3 -- glycogen synthase kinase-3 -- CTFS -- cytosol-soluble peptides containing -- AICD -- APP intracellular domain -- CTFs -- carboxy terminal fragments (CTFs) -- MVEs -- multivesicular endosomes -- ILVs -- intraluminal vesicles -- Alzheimer's disease -- Amyloid -- Presenilin -- Synaptic plasticity -- Neuronal survival -- Endo-lysosomal trafficking -- Cell cycle regulation; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.12.038
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Although widely explored, the pathogenesis of Alzheimer's disease (AD) has yet to be cleared. Over the past twenty years the so call amyloid cascade hypothesis represented the main research paradigm in AD pathogenesis. In spite of its large consensus, the proposed role of β‐amyloid (Aβ) remain to be elucidated. Many evidences are starting to cast doubt on Aβ as the primary causative factor in AD. For instance, Aβ is deposited in the brain following many different kinds of injury. Also, concentration of Aβ needed to induce toxicity in vitro are never reached in vivo . In this review we propose an amyloid‐independent interpretation of several AD pathogenic features, such as synaptic plasticity, endo‐lysosomal trafficking, cell cycle regulation and neuronal survival.