New findings on Global Glial Tauopathy could improve drug design for this pathology
Tauopathies are a group of neurodegenerative diseases known for the accumulation of the phosphorylated Tau protein, i.e. Tau associated with phosphate groups. In this set of pathologies -such as Alzheimerʼs- are glial globular tauopathies, which have an accumulation of phosphor-tau in neurons and the formation of aggregates in glial cells (astrocytes and oligodendrocytes).
Tauopathies are a group of neurodegenerative diseases known for the accumulation of the phosphorylated Tau protein, i.e. Tau associated with phosphate groups. In this set of pathologies -such as Alzheimerʼs- are glial globular tauopathies, which have an accumulation of phosphor-tau in neurons and the formation of aggregates in glial cells (astrocytes and oligodendrocytes).
A new article in the journal Acta Neuropathologica reveals that patients with this tauopathy -spontaneously generated or due genetic mutation- the presence of phosphate groups is not tau-specific but related to many other proteins which are abnormally phosphorylated. This hyperphosphorilation causes the dysfunction and formation of protein deposits causing this neurodegenerative disease.
The study is led by Professor Isidre Ferrer, from the Faculty of Medicine and Health Sciences of the UB, the Bellvitge Institute for Biomedical Research (IDIBELL) and the Bellvitge University Hospital (HUB), in collaboration with Professor José Antonio del Río, from the Faculty of Biology of the UB and the Institute for Bioengineering of Catalonia (IBEC), both members of the Institute of Neurosciences (UBNeuro) of the UB.
According to the new study, in which the Hospital of Navarra took part as well, the accumulation of phosphorylated proteins does not only affect neurons because glial cells (astrocytes and oligodentrocites) are damaged too, a condition that could affect neuronal connections. Moreover, these aggregates are able to move between neurons and glial cells and therefore expand their effects in different areas of the brain as an infection. The new findings open the door to design new drugs to stop the progression of this neurodegenerative disease.
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