They demonstrated that an abnormal form of tau protein, as it occurs in Alzheimer's disease, could be produced in very simple cell models in an unambiguous way.
They also show an example of a chemical compound, found in nature, which is highly effective to completely suppress the abnormal changes of tau.
Researchers have developed a simple cellular assay for the pathological modification of tau protein by abnormal hyperphosphorylation, as seen in Alzheimer's disease and a variety of other neurological disorders (tauopathies).
The assay could be utilized to screen for drugs against these disorders, and the discovery of a very effective small molecule is described as an example.
Tau proteins are a family of neuron-specific proteins thought to play a significant role in the organization of the skeleton of nerve cells.
This protein has been known to be abnormally modified in degenerating neurons in Alzheimer's disease in a process called neurofibrillary degeneration.
And this form of neurodegeneration is believed to be the leading cause of the massive loss of brain mass and function in many dementias, and its inhibition can be expected to change the prognosis of Alzheimer's disease significantly.
Cell models are important tools to examine the molecular mechanisms involved in specific disease processes, and also the mechanisms of drugs, which act against them.
For the process of tau hyperphosphorylation, credible models with utility for drug discovery have not been established to date.
However, the model developed at Sirenade AG under the leadership of Dr. Hanno Roder, fills this important gap.
The study is published in the April issue of the Journal of Alzheimer's Disease.