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Scientists found new direction to treat Alzheimer's disease (AD)!

2017-03-16 来源:亚科官网
16 March 2017
  Researchers from Lund University in Sweden show the physiological conformations of Aβ and amyloid precursor protein (APP) by the synchrotron-based Fourier transform infrared micro-spectroscopy, non-denaturing gel electrophoresis and conformational specific antibodies, which may alter the treatment of Alzheimer's disease.
  Alzheimer disease (AD) is a neurodegenerative disease, mostly in the elderly stage, is the most common disease of dementia. Its clinical manifestations are memory loss, persistent cognitive decline and movement disorders, and accompanied by a series of psychotic symptoms. According to the data from World Health Organization, there are 4,700 million dementia patients, by 2050, it is expected to more than 130 million people.
  In the brain of AD patients, senile plaques of amyloid (Aβ) aggregation occur in the cerebral cortex and hippocampus. Carboxyl terminal of Aβ forms to nuclear factor by self-aggregation, make nuclear factor as the core, the formation of transparent Aβ fibrils happens, and then through a continuous β-fold, the final formation of Aβ fiber occurs. The fiber silk aggregated by Aβ protein has neurotoxicity, it can quickly cause death of a lot of nerve cell. Although Aβ protein is not the only cause of disease, it plays a central role in the development of Alzheimer's disease. The degradation and metabolic disorders of Aβ protein lead to the formation of Aβ protein plaque, which can promote nerve cell apoptosis, activate glial cells, release cytokines and inflammatory mediators, resulting in inflammatory response, accelerate nerve cell death. Moreover, Aβ protein is not only an important factor in the formation of nerve fiber tangles (NFT), but also induce neuronal apoptosis by NFT.
  For a long time, the scientists have always believed that β-amyloid plaques appear instantaneously. The main idea for drug research and development is to regulate Aβ protein production, increase Aβ protein clearance and inhibition of Aβ protein aggregation. Scientists have studied the possible role of tromethamine in AD therapy, which inhibits the gallery formed by Aβ on the membrane, reduces the increase of capacitative calcium entry and increased membrane fluidity caused by Aβ.
  In this study, researchers used the new technique of synchrotron-based Fourier transform infrared micro-spectroscopy, non-denaturing gel electrophoresis and conformational specific antibodies to generate the formation images of toxic clumps prior to beta-amyloid that can be seen closer to Alzheimer's disease in early brain changes. Researchers also found that the progress of β-amyloid protein is slower than we thought, it does not appear suddenly. The results also reveal another major finding: β-amyloid is not a single peptide, which is linked by four peptide units in a tetrameric form. This finding provides a new hypothesis for the treatment of the disease—the abnormal separation of these four peptides may be the beginning of the accumulation of β-amyloid, followed by the formation of plaques.
  Over the years, a large number of experts around the world are working hard to study the treatment of Alzheimer's disease. This new finding may change the direction of our treatment of Alzheimer's disease—by preventing the abnormal separation of these four peptides to prevent the initiation of Aβ aggregation and achieve the goal of treating the disease.
Edited by the Editorial Office of Suzhou Yacoo Science Co., Ltd.