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New protein found could prevent Alzheimer disease

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New protein found could prevent Alzheimer disease

Alzheimer’s disease is the most common form of dementia that affects most frequently people over 65. The most common sign of Alzheimer’s is memory loss, but there can also appear confusion, changes in personality, irritability, urinary incontinence. In advanced stages people with advanced Alzheimer’s can no longer take care of themselves and need special care.

There is no cure for Alzheimer’s disease, which means that once started it cannot be stopped; treatments that exist at present for Alzheimer’s disease are aimed to improve symptoms. Researchers are struggling to find a way to diagnose the disease earlier or rather to prevent the onset of it.

Memory loss occurs due to destruction of neurons which is caused by incorrect folding of proteins in the brain. Now researchers at RIKEN Bioengineering Laboratory in collaboration with the scientists from the Laboratory for Proteolytic Neuroscience at the RIKEN Brain Science Institute, found that the human protein prefoldin can change how these protein aggregates form. They believe this will reduce the harmful effect of these aggregates in the brain.

Alzheimer

Alzheimer

Regarding the causes of Alzheimer’s disease, one of the hypotheses is that of beta-amyloid. The formation of insoluble aggregates of beta-amyloid is considered one of the key mechanisms responsible for the onset of Alzheimer’s disease. It is known that these aggregates are toxic to neurons, so researchers are trying to discover a way to prevent the formation of these. Prefoldin is a molecular chaperone that prevents the wrong packaging of proteins and to help those wrongly packaged to return to normal form. Researchers observed that incubation of beta-amyloid molecules with a small amount of prefoldin can change their behavior: instead of forming insoluble aggregates, prefoldin enabled the formation of soluble beta-amiloid oligomers. Although some researchers believe that amyloid beta oligomers are toxic to neurons, the study shows that certain types of these oligomers are less toxic to neurons.

What researchers noticed was that, like in the brain, beta-amyloid led to the destruction of neurons. Furthermore, experiments on laboratory animals showed that the oligomers formed in the presence of human prefoldin reduced the loss of neurons. Another interesting finding was that prefoldin expression increases with the levels of beta-amyloid, which indicates that there is a mechanism by which the brain is protected by high levels of beta-amyloid. “Our findings may also apply to various other neurological diseases caused by protein misfolding, such as prion disease, Huntington’s disease and Parkinson’s disease,” researchers said.