Alzheimer's is one of the best-known neurodegenerative diseases. It is characterized by difficulties in coordination, tendency to lose objects and memory problems, and ends in total disability and loss of personality. It is in the interest of medical science to find effective ways to treat this disorder, as today, at least 40 million people in the world suffer from it.
However, the most significant difficulty in generating a viable cure has been in determining the causes of death of neurons. Until now, the predominant theory of Alzheimer's etiopathogenesis attributed the greatest responsibility to the beta-amyloid protein. Today, several studies affirm that recombinant TAU proteins are mainly responsible for neuronal death.
The Role of TAU in Alzheimer's Disease
Under normal conditions, the TAU protein is responsible for providing a structure (a kind of highway) within neurons. This structure allows the cells to cleanse themselves, removing accumulations of unwanted proteins and toxins. However, if TAU stops working, a process is triggered that culminates in the death of the cells, eventually producing Alzheimer's, or some other neurodegenerative disease.
This new theory, which gives more weight to TAU in the process, was developed by Charbel E.H. Moussa, from Georgetown University (USA), and published in the journal Molecular Neurodegeneration. According to Moussa: “When TAU does not work, the cell cannot throw away the garbage, which at that moment includes the beta-amyloid protein as well as tangles of tau that does not work and, because of this, the cell dies”. That is, while it is the accumulation of beta-amyloids that eventually causes the cell to die, the primary cause is the alteration of TAU.
How Is TAU Altered?
A group of researchers from the Max Planck Institute for Biophysical Chemistry in Göttingen examined which modules of the TAU protein can act destructively on neurons and influence Alzheimer's disease. According to the study, in its pathogenic form, TAU has more phosphorylated acids than the protein in its standard form. Group leader Markus Zweckstetter focused research on how specific phosphorylated residues alter the structure of the protein so that it no longer binds to microtubules.
Using Nuclear Magnetic Resonance Spectroscopy, the structural properties and movements of TAU could be observed. They could directly see which of the modules of the Tau protein adhere to the microtubules. If the protein is equipped with more phosphates than usual, such binding is significantly weakened.
When the bonds fail, the bridges that link the structure break and stop interacting; this implies that transport through the microtubules is interrupted. As this occurs, the cycle of accumulation described by Moussa in his study begins, initiating the cycle that eventually brings about the destruction of the neuron, and ultimately leads to the neurodegenerative disorder.
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