Friday, August 26, 2016 3:01:40 AM
Anavex 2-73 works by repairing internal damage that has occured in the cell due to stress and also strengthens the cell's internal processes to resist damage. Since it's mode of operation is to get cells functioning again, it doesn't affect cells that are still functioning normally. Clinical trials to date have proven that people have gotten better taking 2-73, improvents over and above and longer than the current standard of care Aricept (donepezil). Donepezil is among a class of drugs that promote accumulation of acetylcholine. This will stimulate a brief increase in neural activity but subsequently has no effect on continued progression of the disease. Unlike 2-73 which is quite safe, boosting acetylcholine can produce undesired side effects. Heart failure is one such listed. Nevertheless, acetylcholine boosters continue to be administered as treatment for Alzheimer's even after they have become completely ineffective.
*AD is currently treated by increasing acetylcholine concentration by using acetylcholinesterase inhibitors to inhibit acetylcholinesterase from breaking down acetylcholine. Current acetylcholinesterase inhibitors approved in the United States by the FDA to treat Alzheimer’s include donepezil, rivastigmine, and galantamine. These drugs work to increase the levels of acetylcholine and subsequently increase the function of neural cells. However, not all treatments based upon the cholinergic hypothesis have been successful in treating the symptoms or slowing the progression of AD. Therefore, a disruption to the cholinergic system has been proposed as a consequence of AD rather than a direct cause.
*Martorana, A; Esposito, Z; Koch, G (August 2010). "Beyond the Cholinergic Hypothesis: Do Current Drugs Work in Alzheimer's Disease?". CNS Neuroscience & Therapeutics. 16 (4): 235–245. doi:10.1111/j.1755-5949.2010.00175.
Now there is a lot of hype and pumping about amyloids and tau "breakthroughs" in the biotech media arena while Anavex continues to be ignored or derided. Even though, like acetylcholine, amyloids and tau have also been a dead end for a long time.
*The expanding interest in dementia has nurtured a worldwide initiative exploring a wide array of disease mechanisms and approaches to treatment. The divergent perspective on the exact cause of this destruction have fostered different theories about what initiates the process and how best to intervene. The theory with the largest following remains the "amyloid hypothesis," which assigns a central role to abnormal pro-cessing of amyloid precursor protein (APP), a protein found widely throughout the body. This abnormal processing yields a fragment called beta-amyloid (Aß), which aggregates by stages into the amyloid plaques that is a hallmark of Alzheimer pathology. Proponents of the amyloid hypothesis see production and aggregation of Aß as the key event in nerve cell disruption and destruction. Neuropathology studies are inconclusive as to the pathogenic role of amyloid in Alzheimer's disease. Quantitative radio immunoassays show that equal amounts of soluble APP are found in the brains of people with Alzheimer's disease and age-matched individuals without Alzheimer's disease, casting doubt on the role of APP. This makes determining the relationship of amyloid to Alzheimer's disease more difficult: dense plaques accumulate with age even in individuals who have no cognitive impairment.
The second most prominent Alzheimer theory assigns a causative role to tau aggregating into neurofibrillary tangles. Many experts remain convinced that understanding tau will reveal crucial clues about Alzheimer’s devastating effects on nerve cells as well as chemical steps vulnerable to intervention. However, there is no conclusive evidence indicating that amyloid plaques and neuro-fibrillary tangles are the cause and not a product of Alzheimer's disease. Plaques and tangles can be observed in the brains of individuals without any detectable form of dementia.
*Snowdon DA., “Aging and Alzheimer's disease: lessons from the Nun study.” Gerontologist 1997; 37(2): 150-156
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