Roles of Aβ and carboxyl terminal peptide fragments of amyloid precursor protein in Alzheimer disease

2000 ◽  
pp. 65-82
Author(s):  
Y.-H. Suh ◽  
H.-S. Kim ◽  
J. P. Lee ◽  
C. H. Park ◽  
S.-J. Jeong ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Peptide Fragments ◽  
Carboxyl Terminal

Etiological roles of A β and carboxyl terminal peptide fragments of amyloid precursor protein in Alzheimer disease

2001 ◽  
pp. 217-224
Author(s):  
Yoo-Hun Suh ◽  
Hye-Sun Kim ◽  
Cheol Hyoung Park ◽  
Ji-Heui Seo ◽  
Jean-Pyo Lee ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Peptide Fragments ◽  
Carboxyl Terminal

G-lymphatic, vascular and immune pathways for Aβ clearance cascade and therapeutic targets for Alzheimer’s disease

2020 ◽  
Vol 23 ◽  
Author(s):  
Saurav Chakraborty ◽  
Jyothsna ThimmaReddygari ◽  
Divakar Selvaraj
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Amyloid Beta ◽  
Complement System ◽  
Therapeutic Targets ◽  
Neuronal Cell ◽  
Precursor Protein ◽  
Amyloid Beta Peptide ◽  
Beta Peptide ◽  
Immune Pathways

The Alzheimer disease is a age related neurodegenerative disease. The factors causing alzheimer disease are numerous. Research on humans and rodent models predicted various causative factors involved in Alzheimer disease progression. Among them, neuroinflammation, oxidative stress and apoptosis play a major role because of accumulation of extracellular amyloid beta peptides. Here, the clearance of amyloid beta peptide plays a major role because of the imbalance in the production and clearance of the amyloid beta peptide. Additionally, neuroinflammation by microglia, astrocytes, cytokines, chemokines and the complement system also have a major role in Alzheimer disease. The physiological clearance pathways involved in amyloid beta peptide are glymphatic, vascular and immune pathways. Amyloid precursor protein, low density lipoprotein receptor-related protein 1, receptor for advanced glycation end product, apolipoprotein E, clusterin, aquaporin 4, auto-antibodies, complement system, cytokines and microglia are involved in amyloid beta peptide clearance pathways across the blood brain barrier. The plaque formation in the brain by alternative splicing of amyloid precursor protein and production of misfolded protein results in amyloid beta agglomeration. This insoluble amyloid beta leads to neurodegenerative cascade and neuronal cell death occurs. Studies had shown disturbed sleep may be a risk factor for dementia and cognitive decline. In this review, the therapeutic targets for alzheimer disease via focussing on pathways for amyloid beta clearance are discussed.

scholarly journals Amyloid Precursor Protein in Platelets of Patients With Alzheimer Disease

2001 ◽  
Vol 58 (3) ◽  
Author(s):  
Barbara Borroni ◽  
Francesca Colciaghi ◽  
Lucia Pastorino ◽  
Carla Pettenati ◽  
Elisabetta Cottini ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Precursor Protein

AMYLOID PRECURSOR PROTEIN IN SENILE PLAQUES OF ALZHEIMER DISEASE

The Lancet ◽  
1988 ◽  
Vol 332 (8613) ◽  
pp. 746 ◽  
Author(s):  
George Perry ◽  
Sandra Lipphardt ◽  
Madhu Kancherla ◽  
Pierluigi Gambetti ◽  
Linda Maggiora ◽  
...  
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Senile Plaques ◽  
Precursor Protein

scholarly journals Investigation of the Iron Oxide Nanoparticle Effects on Amyloid Precursor Protein Processing in Hippocampal Cells

2021 ◽  
Author(s):  
Leila Sadeghi ◽  
◽  
Arezu Marefat ◽  
Keyword(s):  
Iron Oxide ◽  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Magnetic Particles ◽  
Therapeutic Potential ◽  
Precursor Protein ◽  
Neonatal Rat ◽  
Amyloid Precursor Protein Processing ◽  
Iron Oxide Nanoparticle ◽  
Dependent Manner

Introduction: Iron oxide nanoparticles (Fe2O3-NPs) are small magnetic particles that widely used in different aspects of biology and medicine in modern life. Fe2O3-NP accumulated in the living cells due to absence of active system to excrete the iron ions so damages cellular organelles by highly reactivity. Method: Herein cytotoxic effects of Fe2O3-NP with 50 nm size were investigated on primary culture of neonatal rat hippocampus by MTT assay. Pathophysiological signs of Alzheimer disease such as amyloid precursor protein (APP) expression, Aβ aggregation, soluble APPα and APPβ secretion also were investigated in hippocampal cells treated by various concentration of NP for different exposure time. Results: Our results revealed, Fe2O3-NP treatment causes oxidative stress in cells that accompanied by upregulation of the APP and Aβ in a concentration dependent manner. NP exposing also leads to more secretion of sAPPβ rather than sAPPα that concluded to increased activation of β-secretase in NP received cells. All of the harmful effects accumulate in neurons that could not be renovated so lead to neurodegeneration in Alzheimer disease. Conclusion: This study approved iron-based NPs could help to develop the Alzheimer and related neurological disorders and explained why some of the iron chelators have therapeutic potential in Alzheimer disease.

scholarly journals Behavioral and Neuropathologic Changes Induced by Central Injection of Carboxyl-Terminal Fragment of β-Amyloid Precursor Protein in Mice

2002 ◽  
Vol 71 (2) ◽  
pp. 875-878 ◽  
Author(s):  
D.-K. Song ◽  
M.-H. Won ◽  
J.-S. Jung ◽  
J.-C. Lee ◽  
T.-C. Kang ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Terminal Fragment ◽  
Β Amyloid ◽  
Carboxyl Terminal

scholarly journals Rab5-stimulated Up-regulation of the Endocytic Pathway Increases Intracellular β-Cleaved Amyloid Precursor Protein Carboxyl-terminal Fragment Levels and Aβ Production

2003 ◽  
Vol 278 (33) ◽  
pp. 31261-31268 ◽  
Author(s):  
Olivera M. Grbovic ◽  
Paul M. Mathews ◽  
Ying Jiang ◽  
Stephen D. Schmidt ◽  
Ravi Dinakar ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Endocytic Pathway ◽  
Precursor Protein ◽  
Terminal Fragment ◽  
Carboxyl Terminal ◽  
Aβ Production
Sign in / Sign up

Export Citation Format

Share Document