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The study team combined extremely high-resolution microscopy with machine learning to show that tau forms small aggregates as a part of the body’s normal physiology. This potentially opens the door for screening the treatments that might break apart harmful tau aggregates.
‘New method with high-resolution microscopy and machine learning identifies tau aggregates that occur in healthy body structures. Thus further analysis of this potential mechanism for clearing tau aggregates and determine other related pathways could help design treatment for diseases like Alzheimer ?? s disease. ‘
“There aren’t many tools that can visualize small, pathological protein aggregates within cells. But through machine learning informed by super-resolution microscopy, we believe we’ve been able to show that tau forms both normal physiological aggregates and distinct pathological aggregates. In doing so, we created a useful method that could be the basis for new research into the appropriate treatments for tau-related pathologies, ” says the study’s senior author, Melike Lakadamyali, Ph.D., an associate professor of Physiology.
Tau Aggregates and Neurological Diseases
“Intrinsically, there is value in being able to tell which tau aggregates are a part of a healthy person’s nervous system, and which have formed harmful aggregates. Unfortunately, there has not been a process sensitive enough to make that distinction yet inside cells. So we set out to create one using mammalian cell models, ” says the study’s lead author, Melina Theoni Gyparaki, a doctoral student in Lakadamyali’s lab.
With the differences in configuration established, the researchers created a machine-learning algorithm to classify the pathological tau aggregates by shape alone. The study team additionally used antibodies that can detect and differentiate when the tau aggregates become “hyper-phosphorylated” – when they pick up a lot of phosphate groups and tend to harmfully break off.
Thus combining these methods showed that tau containing phosphate groups on certain amino-acids was more likely to form linear fibrils, a thin structure, as opposed to other shapes of tau aggregates.
The method may aid in learning the mechanisms that lead to pathological protein oligomerization in neurodegenerative disease. This may even serve as an opportunity to use it on other potentially pathological protein build-ups, such as alpha-synuclein, which is associated with Parkinson’s disease, or huntingtin, related to Huntington’s disease.
Screening for potential treatments for these conditions that don’t harm the body’s regular protein complexes could also be done using the present method. The team is set to further analyze the potential mechanisms for clearing tau aggregates and determine what other pathways could help explore neurodegenerative diseases.
Source: Medindia
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