Galectin 3–binding protein suppresses amyloid-β production by modulating β-cleavage of amyloid precursor protein
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چکیده
منابع مشابه
AMPA Receptor Activation Promotes Non-Amyloidogenic Amyloid Precursor Protein Processing and Suppresses Neuronal Amyloid-β Production
Soluble oligomeric amyloid β peptide (Aβ) generated from processing of the amyloid precursor protein (APP) plays a central role in the pathogenesis of Alzheimer's Disease (AD) and through actions at glutamatergic synapses affects excitability and plasticity. The physiological control of APP processing is not fully understood but stimulation of synaptic NMDA receptors (NMDAR) can suppress Aβ lev...
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Current therapies for Alzheimer's disease only treat the symptoms of the disease. We have previously developed a novel monoclonal antibody, 2B3, which binds to the β-secretase cleavage site in amyloid precursor protein (APP) and reduces the production of amyloid-β (Aβ) in human cell lines. To determine whether the antibody was likely to be effective in mouse models of amyloid pathology in vivo,...
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Alzheimer's disease (AD) is characterized by disrupted metabolism of the amyloid-β protein precursor (AβPP) and deposition of a byproduct, the amyloid-β (Aβ) peptide, into plaques. AD is also genetically linked to the gene for apolipoprotein E (apoE). We have identified a novel apoE-binding protein (TMCC2) that also forms a complex with AβPP. TMCC2 is a neuronal, predominantly ER-localized, pro...
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BACE1 cleaves the amyloid precursor protein (APP) at the β-cleavage site (Met(671) -Asp(672) ) to initiate the generation of amyloid peptide Aβ. BACE1 is also known to cleave APP at a much less well-characterized β'-cleavage site (Tyr(681) -Glu(682) ). We describe here the identification of a novel APP mutation E682K located at this β'-site in an early onset Alzheimer's disease (AD) case. Funct...
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Alzheimer's disease (AD) is increasingly viewed as a disease of synapses. Loss of synapses correlates better with cognitive decline than amyloid plaques and neurofibrillary tangles, the hallmark neuropathological lesions of AD. Soluble forms of amyloid-β (Aβ) have emerged as mediators of synapse dysfunction. Aβ binds to, accumulates, and aggregates in synapses. However, the anatomical and neuro...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2020
ISSN: 0021-9258
DOI: 10.1074/jbc.ra119.008703