echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Active Ingredient News > Study of Nervous System > Nature: molecular "guard" can help treat Parkinson's disease

    Nature: molecular "guard" can help treat Parkinson's disease

    • Last Update: 2019-12-06
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com
    December 6, 2019 / biourn / - recently, a study published in nature by researchers from the biological center of the University of Basel, Switzerland, revealed the dynamic interaction between chaperones and α - synuclein in human cells The disorder of these interactions will lead to cell damage, which will lead to the occurrence of Parkinson's disease Parkinson's disease is one of the most common neurodegenerative diseases In Switzerland, about 15000 people were affected Due to the increase of life expectancy globally, the number of Parkinson's disease cases is expected to increase rapidly in the next few years The cause of the progressive death of brain neurons is not clear Therefore, it is more difficult to develop effective therapies (image source: www Pixabay Com) it is well known that α - synuclein can play a key role in the development of Parkinson's disease Researchers led by structural biologist Professor Sebastian Hiller have found that chaperones have been protecting alpha synuclein in human cells Whenever chaperones fail to perform their "bodyguard" tasks, alpha synuclein will show its disadvantages and cause serious cell damage In human cells, there are about 30 to 40 molecular chaperones that may interact with alpha synuclein Scientists have systematically studied the atomic level of the interaction between molecular chaperones and α - synuclein "Using state-of-the-art NMR techniques, we found specific patterns for determining the exact site of interaction between alpha synuclein and molecular chaperones," Hiller explained In healthy cells, α - synuclein is always accompanied by chaperone protein, which keeps the protein transportable If partners can no longer perform their bodyguard function, there will be serious consequences Chemical modifications of alpha synuclein, such as those observed in Parkinson's disease, interfere with the binding of molecular chaperones These "unaccompanied" α - synuclein can be relocated and accumulated on the mitochondrial membrane of the cell's power plant, and gradually destroy them "Our research suggests that the role of molecular chaperones goes far beyond protein folding," Hiller said They control cell processes through flexible interactions with a variety of proteins " Riek, Sebastian Hiller Regulation of α-synuclein by chaperones in mammalian cells Nature , 2019; DOI: 10.1038/s41586-019-1808-9
    This article is an English version of an article which is originally in the Chinese language on echemi.com and is provided for information purposes only. This website makes no representation or warranty of any kind, either expressed or implied, as to the accuracy, completeness ownership or reliability of the article or any translations thereof. If you have any concerns or complaints relating to the article, please send an email, providing a detailed description of the concern or complaint, to service@echemi.com. A staff member will contact you within 5 working days. Once verified, infringing content will be removed immediately.

    Contact Us

    The source of this page with content of products and services is from Internet, which doesn't represent ECHEMI's opinion. If you have any queries, please write to service@echemi.com. It will be replied within 5 days.

    Moreover, if you find any instances of plagiarism from the page, please send email to service@echemi.com with relevant evidence.