Green Tea and Red Wine Extracts Reduce Progression of Alzheimer’s Disease

First Posted: Feb 06, 2013 03:03 AM EST

A new way to zap Alzheimer's is incredible. Researchers from the University of Leeds, U.K., have found that the natural compounds present in red wine and green tea reduce the progression of the disease.

Alzheimer's is a type of dementia that attacks 1 in 8 elderly Americans. The disease interferes with daily tasks and gets worse over the passage of time. The victims of Alzheimer's have difficulty in remembering names and recent events, and the disease is one of the leading cause of deaths in the U.S.

In this study, researchers identified a process that permits the harmful cluster of amyloid protein to latch on to the surface of the nerve cells in the brain by clinging on to the proteins on the cell surface called prions. This causes a malfunction in the nerve cells, causing them to die. They interrupted this path, and were successful in stopping the nerve cells from being damaged by using purified extracts of resveratol from red wine and ECGC from green tea.

"This is an important step in increasing our understanding of the cause and progression of Alzheimer's disease. It can be cured through finding new opportunities for drug targets like this," lead researcher professor Nigel Hooper of the University's Faculty of Biological Sciences was quoted as saying in Medicalxpress.

According to Dr. Jo Rushworth, a member of the Leeds team, the team wanted to check whether it was important to know the exact shape of the amyloid balls in order to attach to the prion receptors.  And, if so, they were looking for means to prevent the amyloid balls from binding to prion by changing their shape, as this would end the cells from dying.

The amyloid balls were formed in a test tube and were added to human and animal brain cells. When they added the natural extracts of green tea and red wine that claim to re-shape the amyloid proteins, the researchers noticed that the amyloid balls caused no harm to the nerve cells. This was because the shapes of the proteins were distorted and they failed to bind to the prion and cause any malfunction.

For the first time, this study showed how amyloid balls stick to prion and activates the production of extra amyloid, in a deadly vicious cycle.

Next, the team aims at understanding how the amyloid prion interaction destroys the neurons.

The study was published in the Journal of Biological Chemistry.

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