The International Research Group, led by the University of Würzburg (Germany), has demonstrated a critical mechanism used by cells to remove harmful protein clusters. These proteins provoke the development of various neurodegenerative diseases. The study was published scientifically magazine Nature Communication (Natcoms).
The team learned that the P97/VCP enzyme (Kilquitin-Sectative Anfoldase) plays a central role in the destruction of protein units known as aggressive. These incorrectly curled protein accumulation occurs with neurodegenerative diseases and should normally be removed by a cell. However, if the P97/VCP is blocked, the cleaning process is disrupted, which leads to the accumulation of toxic deposits.
“Without this enzyme, aggressives are not divided and displayed into smaller components. This may be one of the reasons for the progression of diseases associated with protein aggregation,” he explained.
Mutations in P97/VCP are already known as the cause of some dementia forms and lateral amyotrophic sclerosis (bass). In the case of Parkinson’s illness in neurons, Taurus Levy forms – the accumulation of protein that can be “unstable” aggressomes as suggested by scientists.
New data confirm that P97/VCP dysfunction contributes to the development of these pathologies by violating the natural process of cell therapy.
The discovery leads to the development of drugs that can activate P97/VCP to increase the deterioration of harmful proteins.
Previously, scientists open Connection between schizophrenia and accelerated brain aging.
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Source: Gazeta
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