Amyloid β-peptide alters thrombin-induced calcium responses in cultured human neural cells

Amyloid ◽  
1996 ◽  
Vol 3 (1) ◽  
pp. 28-40 ◽  
Author(s):  
Mark P Mattson ◽  
James G. Begley
Keyword(s):  
Amyloid Β ◽  
Neural Cells ◽  
Amyloid Β Peptide ◽  
Human Neural Cells

Potential of medicinal plants as neuroprotective and therapeutic properties against amyloid-β-related toxicity, and glutamate-induced excitotoxicity in human neural cells

2021 ◽  
Vol 19 ◽  
Author(s):  
Devina Lobine ◽  
Nabeelah Sadeer ◽  
Sharmeen Jugreet ◽  
Shanoo Suroowan ◽  
Bibi Sumera Keenoo ◽  
...  
Keyword(s):  
Plant Species ◽  
Neuronal Cell Death ◽  
Amyloid Β ◽  
Neuronal Cell ◽  
Neural Cells ◽  
Amyloid Β Peptide ◽  
Limited Effectiveness ◽  
Baseline Information ◽  
Approved Drugs ◽  
Pharmacologically Active

: Alzheimer’s disease (AD) and Parkinson disease (PD) are notorious neurodegenerative diseases amongst the general population. Being age-associated diseases, the prevalence of AD and PD is forecasted to rapidly escalate with the progressive aging population of the world. These diseases are complex and multifactorial. Among the different events, amyloid β peptide (Aβ) induced toxicity is a well‐established pathway of neuronal cell death which plays a vital function in AD. Glutamate, the major excitatory transmitter, acts a neurotoxin when present in excess at the synapses; this latter mechanism is termed as excitotoxicity. It is hypothesised that glutamate-induced excitotoxicity contributes to the pathogenesis of AD and PD. No cure for AD and PD is currently available and the currently approved drugs available to treat these diseases have limited effectiveness and pose adverse effects. Indeed, plants have been a major source for the discovery of novel pharmacologically active compounds for distinct pathological conditions. Diverse plant species employed for brain related disorders in the traditional medicine are being explored to determine them scientific rationale behind their uses. Herein, we present a comprehensive review of plants and their constituents have shown promise in reversing the (i) amyloid-β -related toxicity in AD models and (ii) glutamate-induced excitotoxicity in AD and PD models. This review summarizes information with regard to the phytochemistry, biological and cellular activities as well as clinical trials of several plant species in view to provide adequate scientific baseline information that could be used in drug development process, thereby providing effective leads for AD and PD.

Protein kinase C iota protects neural cells against apoptosis induced by amyloid β-peptide

2000 ◽  
Vol 82 (1-2) ◽  
pp. 107-113 ◽  
Author(s):  
Jun Xie ◽  
Qing Guo ◽  
Haiyan Zhu ◽  
Marie W Wooten ◽  
Mark P Mattson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Amyloid Β ◽  
Neural Cells ◽  
Amyloid Β Peptide ◽  
Kinase C ◽  
Protein Kinase C Iota

scholarly journals Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells

2007 ◽  
Vol 13 (10) ◽  
pp. 953-969 ◽  
Author(s):  
C Schmidt ◽  
E Lepsverdize ◽  
S L Chi ◽  
A M Das ◽  
S V Pizzo ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Atp Synthase ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Neural Cells ◽  
Amyloid Β Peptide

scholarly journals Alzheimer’s Presenilin Mutation Sensitizes Neural Cells to Apoptosis Induced by Trophic Factor Withdrawal and Amyloid β-Peptide: Involvement of Calcium and Oxyradicals

1997 ◽  
Vol 17 (11) ◽  
pp. 4212-4222 ◽  
Author(s):  
Qing Guo ◽  
Bryce L. Sopher ◽  
Katsutoshi Furukawa ◽  
Dao G. Pham ◽  
Nic Robinson ◽  
...  
Keyword(s):  
Amyloid Β ◽  
Trophic Factor ◽  
Neural Cells ◽  
Amyloid Β Peptide

Amyloid β-peptide and Alzheimer's disease

2014 ◽  
Vol 56 ◽  
pp. 99-110 ◽  
Author(s):  
David Allsop ◽  
Jennifer Mayes
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Senile Plaques ◽  
Strong Support ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Amyloid Cascade Hypothesis ◽  
Sequence Of Events ◽  
Aβ Amyloid ◽  
Amyloid Cascade

One of the hallmarks of AD (Alzheimer's disease) is the formation of senile plaques in the brain, which contain fibrils composed of Aβ (amyloid β-peptide). According to the ‘amyloid cascade’ hypothesis, the aggregation of Aβ initiates a sequence of events leading to the formation of neurofibrillary tangles, neurodegeneration, and on to the main symptom of dementia. However, emphasis has now shifted away from fibrillar forms of Aβ and towards smaller and more soluble ‘oligomers’ as the main culprit in AD. The present chapter commences with a brief introduction to the disease and its current treatment, and then focuses on the formation of Aβ from the APP (amyloid precursor protein), the genetics of early-onset AD, which has provided strong support for the amyloid cascade hypothesis, and then on the development of new drugs aimed at reducing the load of cerebral Aβ, which is still the main hope for providing a more effective treatment for AD in the future.

Insights into amyloid disease from fly models

2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther
Keyword(s):  
Drosophila Melanogaster ◽  
Neurodegenerative Disorders ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Disease Pathogenesis ◽  
Amyloid Aggregates ◽  
Aβ Amyloid ◽  
Polypeptide Chains ◽  
Amyloid Diseases

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.

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