Neurodegenerative diseases are a real pain for humanity. A lot of people, especially elders, are suffering from it. Nothing seems to be more dreadful than losing your memory and ability to think logically and rationally, so researchers are significantly struggling to find efficient cures and medication.
Around 50 million Americans are affected each year by this type of diseases, and there are over 600 neurological disorders. The tau protein, which is found abundantly in neurons, is believed by scientists to be a major culprit for neurodegenerative diseases. Therefore, trying to understand more about tau could be the key for developing better treatments for the disorders.
The purpose of the tau protein
The tau protein has the mission to maintain structure and stability within neurons, as it helps by transporting nutrients from one part of the brain cell to another. But the protein can also misfold, becoming deadly for the neurons. The misfolded tau protein can further be transmitted from one cell to another.
Researchers believe that if the spread of pathological tau protein is caught early enough, the neurodegenerative disease can be stopped from progressing, and thus the patient will have a normal life.
In a paper published in the journal Nature, a team of researchers has uncovered a pattern by which the tau protein travels from one brain cell to another. The discovery yields a way to control the spread of the ‘bad tau’, as well as providing extra info about the propagation of the protein when it comes to neurodegenerative diseases.
The LRP1 lipoprotein is a key factor
The researchers involved discovered that the key factor for the pattern of spreading the ‘unwanted guest’ is the LRP1 lipoprotein. It’s involved in some processes, like helping the brain cell take in some necessary substances.
Kosik is the Harriman Professor of Neuroscience Research in UC Santa Barbara’s Department of Molecular, Cellular, and Developmental Biology. He declared:
“This protein is an interesting one in its own right because it’s a little bit like an extracellular trash can,”
“It doesn’t just pick up tau; if there’s other rubbish out there, it also picks it up.”
The study’s lead author, postdoctoral researcher Jennifer Rauch, said about the new findings:
“Since our cellular work showed that tau can interact with the cell-surface receptor LRP1 and that this causes tau’s endocytosis, our hypothesis was that if we reduce LRP1 expression in the mice we should reduce the ability for neighboring neurons to take up tau,”
However, further work is needed to clear any doubts. Neurodegenerative diseases are not incurable, and new tools for fighting them are already looming.