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The One Kind Of Stress That’s Good For The Brain

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You know that too much stress is bad for your body and your brain. Over the long term, a high-stress lifestyle can lead to anxiety, chronic inflammation, obesity and even cancer. However, the latest research shows that a little of the right kind of stress can actually improve your memory and help your brain rejuvenate itself. One expert describes the new discovery as a game-changer in memory preservation... In a healthy person, proteins are formed and then folded in the brain to create a stable three-dimensional structure that’s essential for normal cognitive function. Misfolded proteins at best will be inactive and at worse will become toxic. The brain has its own quality control mechanisms to ensure proteins are folded correctly or destroyed if they’re not. But in neurodegenerative diseases this process becomes impaired and can lead to a buildup of misfolded proteins like amyloid and tau – the hallmarks of Alzheimer’s disease. Scientists at the UK Dementia Research Institute, University of Cambridge, wanted to find out if stressing part of a cell would lead to protein misfolding. What they discovered came as a total, but welcome, surprise.

Misfolded Proteins Are Refolded and Restored 

Just as it seems we can become more alert and benefit from a small amount of healthy stress, yet we‘re negatively affected from overwork, cells react in the same way. For example, a little stress helps cells produce proteins in response to an infection, but they also get overburdened if forced to produce a large number of proteins to deal with too much stress such as extremes of temperature, toxins, free radicals, DNA damage, infections and other challenges. Using lab grown cells, the scientists deliberately stressed a membrane structure called the endoplasmic reticulum (ER) which produces a third of proteins and is a central player in many of their key functions. They fully expected ER stressing would lead to protein misfolding and clumping and this would explain why so many beta-amyloid plaques are formed in the brains of dementia patients. Joint study supervisor Dr. Edward Avezov describes how their theory was not just disproved but turned on its head. “We were astonished to find that stressing the cell actually eliminated the aggregates – not by degrading them or clearing them out, but by unravelling the aggregates, potentially allowing them to refold correctly. Dr. Avezov is hopeful their new discovery will open the doors to finding new treatments for Alzheimer’s disease by triggering this natural process in cells. “If we can find a way of awakening this mechanism without stressing the cells – which could cause more damage than good – then we might be able to find a way of treating some dementias.” He also speculated that the mechanism for how this occurs could be linked to the brain benefits of a sauna bath.

The Brain Benefits of Heat Shock Proteins 

Researchers discovered that a class of proteins called heat shock proteins (HSPs) are a major factor in the protein refolding mechanism. These HSPs respond to stress from higher-than-normal temperatures. Dr. Avezov explains, saying, “There have been some studies recently of people in Scandinavian countries who regularly use saunas suggesting that they may be at lower risk of developing dementia. “One possible explanation for this is that this mild stress triggers a higher activity of HSPs, helping correct tangled proteins.”

New Hope For Alzheimer’s Patients 

One expert who is excited by this breakthrough study is Dr. Richard Oakley, Associate Director of Research at the Alzheimer’s Society. He believes that even though still at its early stages, it’s a “game-changer for dementia research” and a “step towards effective and safe treatments”. Of course, another expert neurologist warned us not to get our hopes up for a treatment any time soon. Professor Tara Spires-Jones from the University of Edinburgh, said that “a drug which targets these mechanisms is likely to be many years away.”
  1. of-toxic-proteins-in-dementia
  2. protein-build-up 

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