scholarly journals Highly increased CSF tau protein and decreased beta-amyloid (1-42) in sporadic CJD: a discrimination from Alzheimer's disease?

2001 ◽  
Vol 71 (3) ◽  
pp. 401-403 ◽  
Author(s):  
E Kapaki
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Beta Amyloid ◽  
Sporadic Cjd

scholarly journals Bioassay-Guided Isolation of Neuroprotective Compounds fromUncaria rhynchophyllaagainst Beta-Amyloid-Induced Neurotoxicity

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Yan-Fang Xian ◽  
Zhi-Xiu Lin ◽  
Qing-Qiu Mao ◽  
Zhen Hu ◽  
Ming Zhao ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Intracellular Calcium ◽  
Pc12 Cells ◽  
Tau Protein ◽  
Beta Amyloid ◽  
Active Ingredients ◽  
Uncaria Rhynchophylla ◽  
Model Of Alzheimer’S Disease ◽  
Calcium Overloading

Uncaria rhynchophyllais a component herb of many Chinese herbal formulae for the treatment of neurodegenerative diseases. Previous study in our laboratory has demonstrated that an ethanol extract ofUncaria rhynchophyllaameliorated cognitive deficits in a mouse model of Alzheimer’s disease induced by D-galactose. However, the active ingredients ofUncaria rhynchophyllaresponsible for the anti-Alzheimer’s disease activity have not been identified. This study aims to identify the active ingredients ofUncaria rhynchophyllaby a bioassay-guided fractionation approach and explore the acting mechanism of these active ingredients by using a well-established cellular model of Alzheimer’s disease, beta-amyloid- (Aβ-) induced neurotoxicity in PC12 cells. The results showed that six alkaloids, namely, corynoxine, corynoxine B, corynoxeine, isorhynchophylline, isocorynoxeine, and rhynchophylline were isolated from the extract ofUncaria rhynchophylla. Among them, rhynchophylline and isorhynchophylline significantly decreased Aβ-induced cell death, intracellular calcium overloading, and tau protein hyperphosphorylation in PC12 cells. These results suggest that rhynchophylline and isorhynchophylline are the major active ingredients responsible for the protective action ofUncaria rhynchophyllaagainst Aβ-induced neuronal toxicity, and their neuroprotective effect may be mediated, at least in part, by inhibiting intracellular calcium overloading and tau protein hyperphosphorylation.

scholarly journals Intensive protein synthesis in neurons and phosphorylation of beta-amyloid precursor protein and tau-protein are triggering factors of neuronal amyloidosis and Alzheimer's disease

2013 ◽  
Vol 59 (2) ◽  
pp. 144-170 ◽  
Author(s):  
A.V. Maltsev ◽  
N.V. Dovidchenko ◽  
V.K. Uteshev ◽  
V.V. Sokolik ◽  
O.M. Shtang ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Synthesis ◽  
Amyloid Precursor Protein ◽  
Tau Protein ◽  
Beta Amyloid ◽  
Precursor Protein ◽  
Tau Proteins ◽  
Neuron Death ◽  
Protective Mechanisms

Recently the studies of Alzheimer’s disease have become particularly actual and have attracted scientists from all over the world to this problem as a result of dissemination of this dangerous disorder. The reason for such pathogenesis is not known, but the final image, for the first time obtained on microscopic brain sections from patients with this disease more than a hundred years ago, is well known to clinicists. This is the deposition of Ab amyloid in the brain tissue of senile plaques and fibrils. Many authors suppose that the deposition of beta-amyloid provokes secondary neuronal changes which are the reason of neuron death. Other authors associate the death of neurons with hyperphosphorylation of tau-proteins which form neurofibrillar coils inside nerve cells and lead to their death. For creation of methods of preclinical diagnostics and effective treatment of Alzheimer’s disease novel knowledge is required on the nature of triggering factors of sporadic isoforms of Alzheimer’s disease, on cause-effect relationships of phosphorylation of amyloid precursor protein with formation of pathogenic beta-amyloids, on the relationship with these factors of hyperphosphorylation of tau-protein and neuron death. In this review we analyze the papers describing the increasing of intensity of biosynthesis in neurons in normal conditions and under the stress, the possibility of development of energetic unbalanced neurons and activation of their protective systems. Phosphorylation and hyperphosphorylation of tau-proteins is also tightly connected with protective mechanisms of cells and with processes of evacuation of phosphates, adenosine mono-phosphates and pyrophosphates from the region of protein synthesis. Upon long and high intensity of protein synthesis the protective mechanisms are overloaded and the complementarity of metabolitic processes is disturbed. This results in dysfunction of neurons, transport collapse, and neuron death.

P3-085: Interaction network of tau protein, beta-amyloid protein, and amyloid protein precursor under oxidative stress in Alzheimer's disease

2015 ◽  
Vol 11 (7S_Part_14) ◽  
pp. P651-P652
Author(s):  
Eduardo de SouzaS. Nicolau ◽  
Ana Paula Mendes Silva ◽  
Kenia Kelly Fiaux do Nascimento ◽  
Kelly Silva Pereira ◽  
Gizele Ribeiro dos Santos ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Interaction Network ◽  
Beta Amyloid ◽  
Amyloid Protein ◽  
Protein Precursor ◽  
Amyloid Protein Precursor ◽  
Beta Amyloid Protein

P4-001: CHANGES IN FRONTOCORTICAL INTERSTITIAL FLUID LEVELS OF BETA-AMYLOID AND TAU PROTEIN IN TRANSGENIC MICE MODELS OF ALZHEIMER'S DISEASE

2014 ◽  
Vol 10 ◽  
pp. P784-P784
Author(s):  
Alain Gobert ◽  
Gaelle Rollin-Jego ◽  
Fabrice Iop ◽  
Jean Michel Rivet ◽  
Dominique Favale ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Transgenic Mice ◽  
Tau Protein ◽  
Interstitial Fluid ◽  
Beta Amyloid ◽  
Fluid Levels

O2-02-01: Prediction of Alzheimer's disease by beta-amyloid plaques and tau protein in frontal cortical biopsy

2010 ◽  
Vol 6 ◽  
pp. S97-S97
Author(s):  
Ville Leinonen ◽  
Anne M. Koivisto ◽  
Jaana Rummukainen ◽  
Juuso Tamminen ◽  
Tomi Tillgren ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Amyloid Plaques ◽  
Beta Amyloid

scholarly journals Role of Withaferin A and Its Derivatives in the Management of Alzheimer’s Disease: Recent Trends and Future Perspectives

Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3696
Author(s):  
Rajib Das ◽  
Abdur Rauf ◽  
Saima Akhter ◽  
Mohammad Nazmul Islam ◽  
Talha Bin Emran ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Therapeutic Potential ◽  
Biological Effects ◽  
Amyloid Plaque ◽  
Beta Amyloid ◽  
Withaferin A ◽  
Protein Accumulation ◽  
Age Related

Globally, Alzheimer’s disease (AD) is one of the most prevalent age-related neurodegenerative disorders associated with cognitive decline and memory deficits due to beta-amyloid deposition (Aβ) and tau protein hyperphosphorylation. To date, approximately 47 million people worldwide have AD. This figure will rise to an estimated 75.6 million by 2030 and 135.5 million by 2050. According to the literature, the efficacy of conventional medications for AD is statistically substantial, but clinical relevance is restricted to disease slowing rather than reversal. Withaferin A (WA) is a steroidal lactone glycowithanolides, a secondary metabolite with comprehensive biological effects. Biosynthetically, it is derived from Withania somnifera (Ashwagandha) and Acnistus breviflorus (Gallinero) through the mevalonate and non-mevalonate pathways. Mounting evidence shows that WA possesses inhibitory activities against developing a pathological marker of Alzheimer’s diseases. Several cellular and animal models’ particulates to AD have been conducted to assess the underlying protective effect of WA. In AD, the neuroprotective potential of WA is mediated by reduction of beta-amyloid plaque aggregation, tau protein accumulation, regulation of heat shock proteins, and inhibition of oxidative and inflammatory constituents. Despite the various preclinical studies on WA’s therapeutic potentiality, less is known regarding its definite efficacy in humans for AD. Accordingly, the present study focuses on the biosynthesis of WA, the epidemiology and pathophysiology of AD, and finally the therapeutic potential of WA for the treatment and prevention of AD, highlighting the research and augmentation of new therapeutic approaches. Further clinical trials are necessary for evaluating the safety profile and confirming WA’s neuroprotective potency against AD.

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