scholarly journals Alterations of Mitochondria and Golgi Apparatus Are Related to Synaptic Pathology in Alzheimer's Disease

10.5772/56079 ◽  
2013 ◽  
Author(s):  
Stavros J.
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Golgi Apparatus ◽  
Synaptic Pathology

P2-101: EVALUATION OF THE PRESYNAPTIC PROTEIN SNAP-25 AS A NOVEL CEREBROSPINAL FLUID MARKER FOR SYNAPTIC PATHOLOGY IN ALZHEIMER'S DISEASE

2014 ◽  
Vol 10 ◽  
pp. P508-P508
Author(s):  
Annika Öhrfelt ◽  
Gunnar Brinkmalm ◽  
William G. Honer ◽  
Lutz Frölich ◽  
Lucrezia Hausner ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cerebrospinal Fluid ◽  
Synaptic Pathology ◽  
Presynaptic Protein

scholarly journals Inhibition of 37/67kDa Laminin-1 Receptor Restores APP Maturation and Reduces Amyloid-β in Human Skin Fibroblasts from Familial Alzheimer’s Disease

2020 ◽  
Vol 10 (4) ◽  
pp. 232
Author(s):  
Antaripa Bhattacharya ◽  
Antonella Izzo ◽  
Nunzia Mollo ◽  
Filomena Napolitano ◽  
Adriana Limone ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Golgi Apparatus ◽  
Protein Misfolding ◽  
Neurodegenerative Disorder ◽  
Amyloid Β ◽  
Laminin Receptor ◽  
Mitochondrial Network ◽  
App Trafficking ◽  
Healthy Control

Alzheimer’s disease (AD) is a fatal neurodegenerative disorder caused by protein misfolding and aggregation, affecting brain function and causing dementia. Amyloid beta (Aβ), a peptide deriving from amyloid precursor protein (APP) cleavage by-and γ-secretases, is considered a pathological hallmark of AD. Our previous study, together with several lines of evidence, identified a strict link between APP, Aβ and 37/67kDa laminin receptor (LR), finding the possibility to regulate intracellular APP localization and maturation through modulation of the receptor. Here, we report that in fibroblasts from familial AD (fAD), APP was prevalently expressed as an immature isoform and accumulated preferentially in the transferrin-positive recycling compartment rather than in the Golgi apparatus. Moreover, besides the altered mitochondrial network exhibited by fAD patient cells, the levels of pAkt and pGSK3 were reduced in respect to healthy control fibroblasts and were accompanied by an increased amount of secreted Aβ in conditioned medium from cell cultures. Interestingly, these features were reversed by inhibition of 37/67kDa LR by NSC47924 a small molecule that was able to rescue the “typical” APP localization in the Golgi apparatus, with consequences on the Aβ level and mitochondrial network. Altogether, these findings suggest that 37/67kDa LR modulation may represent a useful tool to control APP trafficking and Aβ levels with implications in Alzheimer’s disease.

scholarly journals Dysfunction of the ubiquitin ligase E3A Ube3A/E6-AP contributes to synaptic pathology in Alzheimer’s disease

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Markel Olabarria ◽  
Silvia Pasini ◽  
Carlo Corona ◽  
Pablo Robador ◽  
Cheng Song ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Ubiquitin Ligase ◽  
Synaptic Pathology

Presenilin mutations linked to familial Alzheimer's disease reduce endoplasmic reticulum and Golgi apparatus calcium levels

Cell Calcium ◽  
2006 ◽  
Vol 39 (6) ◽  
pp. 539-550 ◽  
Author(s):  
Giancarlo Zatti ◽  
Andrea Burgo ◽  
Marta Giacomello ◽  
Laura Barbiero ◽  
Roberta Ghidoni ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Familial Alzheimer’S Disease ◽  
Familial Alzheimer's Disease

Immunoelectron microscopic study of synaptic pathology in Alzheimer's disease

1991 ◽  
Vol 81 (4) ◽  
pp. 428-433 ◽  
Author(s):  
E. Masliah ◽  
L. Hansen ◽  
T. Albright ◽  
M. Mallory ◽  
R. D. Terry
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Microscopic Study ◽  
Synaptic Pathology
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