A new breakthrough in the research on the pathogenesis of Alzheimer's disease
August 24, 2015 Source: Xinhuanet
Window._bd_share_config={ "common":{ "bdSnsKey":{ },"bdText":"","bdMini":"2","bdMiniList":false,"bdPic":"","bdStyle":" 0","bdSize":"16"},"share":{ }};with(document)0[(getElementsByTagName('head')[0]||body).appendChild(createElement('script')) .src='http://bdimg.share.baidu.com/static/api/js/share.js?v=89860593.js?cdnversion='+~(-new Date()/36e5)];Alzheimer's disease is a neurodegenerative disease. The clinical manifestation is the appearance of amyloid plaques in brain tissue sections. The neurons gradually die, the cognitive and memory abilities are impaired, the patients gradually lose their independent living ability, and finally the brain function is seriously impaired until death. . The statistical results show that the number of people suffering from the disease in China is as high as 5 million, accounting for about a quarter of the total number of patients in the world. Due to the lack of preventive and therapeutic means and the lack of special effects drugs, the disease gradually has an increasing age of onset and an increase in the number of cases.
Current research has shown that the occurrence of Alzheimer's disease is closely related to the formation of amyloid plaques in the brain. The formation of amyloid plaques is in turn associated with protein gamma secretase, which causes the onset of Alzheimer's disease. The gamma secretase consists of four subunits, one of which is presenilin. More than 200 mutations are known to cause dysfunction of presenilin or gamma secretase, causing Alzheimer's disease.
A few days ago, Shi Yigong's research team calculated the three-dimensional structure of γ-secretase with a resolution of 3.4 angstroms. The resolution of 3.4 angstroms makes it possible to observe the side chain of most amino acids as well as the partial glycosylation and binding of lipid molecules in the extracellular domain.
This research advance is important for determining the location of genetic mutations that cause Alzheimer's disease. On the basis of the high-resolution structure, Shi Yigong's research team studied the pathogenic mutants of presenilin and found that these mutations were mainly concentrated in two relatively concentrated regions, namely transmembrane regions TM2-5 and TM6. -9. They studied the biochemical properties of some of the mutants and found that these mutations have different effects on the enzymatic activity of γ-secretase, so a new topic has been proposed for the pathogenesis of existing Alzheimer's disease.
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