Green tea and red wine purified extracts interrupt a vital step in the disease process
One in eight older American’s has Alzheimer’s disease. Alzheimer’s disease is the sixth leading cause of death in the United States, according to the Alzheimer’s association.
Alzheimer’s disease is defined by an apparent build-up of amyloid protein in the brain that bundle together to form toxic, sticky balls of varying shapes. These amyloid balls latch on to the surface of nerve cells in the brain by attaching to proteins on the cell surface called prions, causing the nerve cells to malfunction and eventually die.
Dr. Jo Rushworth, Research Fellow, School of Biomedical Sciences, University of Leeds and co-author of this study explains “We wanted to investigate whether the precise shape of the amyloid balls is essential for them to attach to the prion receptors, like the way a baseball fits snugly into its glove.” "And if so, we wanted to see if we could prevent the amyloid balls binding to prion by altering their shape, as this would stop the cells from dying."
In early stage laboratory experiments, the research team determined the process that allows damaging clumps of protein in which fasten on the brain cells results in death of the cells. Researchers used purified extracts to see if they could interrupt the pathway. The extracts used were ECGC from Green tea and resveratrol from red wine.
In past studies ECGC has been shown to significantly provide protection against amyloid plaque formation. When it comes to resveratrol past research has suggested that resveratrol may help in the removal of amyloid.
For the study researchers formed amyloid balls in test tubes and then added the amyloid balls to human and animal brain cells.
Professor Nigel Hooper, PhD, Professor of Biochemistry, School of Molecular and Cellular Biology at Leeds and lead researcher commented “When we added the extracts from red wine and green tea, which recent research has shown to re-shape amyloid proteins, the amyloid balls no longer harmed the nerve cells. We saw that this was because their shape was distorted, so they could no longer bind to prion and disrupt cell function.” "We also showed, for the first time, that when amyloid balls stick to prion, it triggers the production of even more amyloid, in a deadly vicious cycle.”
Professor Hooper says the next step for the research team is to understand exactly how the amyloid-prion interaction kills off neurons.
In closing Professor Hooper comments "I'm certain that this will increase our understanding of Alzheimer's disease even further, with the potential to reveal yet more drug targets.”
Dr. Simon Riley, PhD, Head of Research at Alzheimer's Research UK commented in part about the study, “While these early-stage results should not be a signal for people to stock up on green tea and red wine, they could provide an important new lead in the search for new and effective treatments.”
This study is published in the Journal of Biological Chemistry.
The research was funded by the Wellcome Trust, Alzheimer's Research UK and the Medical Research Council.
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The other researchers on the team were Heledd H. Griffith and Dr. Nicole Watt, PhD, from the University of Leeds.
Alzheimer's disease is the most common cause of dementia, affecting around 496,000 people in the UK.
As of 2010, there are an estimated 36 million people worldwide with dementia. Nearly two thirds of them live in developing countries. This figure is set to increase to more than 115 million people by 2050, according to Alzheimer’s Disease International.
More information on Alzheimer’s disease can be found online at the Alzheimer’s Association.
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