The resveratrol trimer miyabenol C inhibits β-secretase activity and β-amyloid generation.
PLoS ONE, 2015 Accumulation and deposition of amyloid-β peptide (Aβ) in the brain is a primary cause of the pathogenesis of Alzheimer's disease (AD). Aβ is generated from amyloid-β precursor protein (APP) through sequential cleavages first by β-secretase and then by γ ...
Jin Hu +9 more
doaj +1 more source
LRP1 Has a Predominant Role in Production over Clearance of Aβ in a Mouse Model of Alzheimer's Disease. [PDF]
, 2019 The low-density lipoprotein receptor-related protein-1 (LRP1) has a dual role in the metabolism of the amyloid precursor protein (APP). In cellular models, LRP1 enhances amyloid-β (Aβ) generation via APP internalization and thus its amyloidogenic ...
Gordts, Philip LSM +7 more
core +3 more sources
β‐secretase‐cleaved amyloid precursor protein in Alzheimer brain: a morphologic study [PDF]
Journal of Cellular and Molecular Medicine, 2004 Abstractβ‐amyloid (Aβ) is the main constituent of senile plaques seen in Alzheimer's disease. Aβ is derived from the amyloid precursor protein (APP) via proteolytic cleavage by proteases β‐ and β‐secretase. In this study, we examined content and localization of β‐secretase‐cleaved APP (β‐sAPP) in brain tissue sections from the frontal, temporal and ...
Sennvik, Kristina +4 more
openaire +3 more sources
Presenilin 2 is the predominant γ-secretase in microglia and modulates cytokine release. [PDF]
PLoS ONE, 2010 Presenilin 1 (PS1) and Presenilin 2 (PS2) are the enzymatic component of the γ-secretase complex that cleaves amyloid precursor protein (APP) to release amyloid beta (Aβ) peptide.
Suman Jayadev +8 more
doaj +1 more source
Signal peptide peptidases and gamma-secretase: Cousins of the same protease family? [PDF]
, 2007 Signal peptide peptidase (SPIP) is an unusual aspartyl protease, which mediates clearance of signal peptides by proteolysis within the endoplasmic reticulum (ER).
Christian Haass +15 more
core +2 more sources
-Secretase-Regulated Signaling Mechanisms: Notch and Amyloid Precursor Protein [PDF]
, 2012 In Drosophila, Notch mutations lost a lateral signaling ability and produced a neurogenic phenotype, where cells destined to become epidermis switch fate and give rise to neural tissue (Artavanis-Tsakonas et al. 1995; Lewis 1998). Therefore, when Notch signaling was disrupted, too many neurons were generated.
Nakayama, Kohzo +3 more
openaire +2 more sources
Cellular prion protein regulates β-secretase cleavage of the Alzheimer's amyloid precursor protein [PDF]
Proceedings of the National Academy of Sciences, 2007 Proteolytic processing of the amyloid precursor protein (APP) by β-secretase, β-site APP cleaving enzyme (BACE1), is the initial step in the production of the amyloid β (Aβ) peptide, which is involved in the pathogenesis of Alzheimer's disease.
Parkin, Ed +8 more
openaire +3 more sources
Regulation of amyloid precursor protein processing by serotonin signaling. [PDF]
PLoS ONE, 2014 Proteolytic processing of the amyloid precursor protein (APP) by the β- and γ-secretases releases the amyloid-β peptide (Aβ), which deposits in senile plaques and contributes to the etiology of Alzheimer's disease (AD). The α-secretase cleaves APP in the
Anna A Pimenova +3 more
doaj +1 more source
Biology Open, 2021 The organic anion transporter Adenosine triphosphate binding cassette subfamily C member 1 (ABCC1), also known as MRP1, has been demonstrated in murine models of Alzheimer's disease (AD) to export amyloid beta (Abeta) from the endothelial cells of the ...
Wayne M. Jepsen +7 more
doaj +1 more source
Neuronal human BACE1 knock-in induces systemic diabetes in mice [PDF]
, 2016 Acknowledgements The authors thank S. Tammireddy (Diabetes and Cardiovascular Science, University of the Highlands and Islands, Inverness, UK) for technical support with the lipidomics component. Funding We would like to thank R.
Dekeryte, Ruta +12 more
core +4 more sources