Research done by scientists at the Instituto de Neurociencias de Alicante, in Spain has revealed that the way people with Alzheimer’s process a key protein may lead to the creation of new tests and maybe even treatments. Alzheimer’s disease is a common form of dementia, where memory and thinking skills are progressively lost.
People with Alzheimers have a build up of insoluble plaques made of beta-amyloid and tau, both are proteins. Beta-amyloid is a part of a much larger protein called amyloid precursor protein, which is otherwise known as APP. APP is broken down by enzymes into either a beta-amyloid fragment, which is harmful, and causes Alzheimers, or another harmless fragment.
Glycosylation is the process of adding sugars to proteins, to form a glycoprotein, during production and the location of these sugar molecules is important in determining the ultimate destination of the protein in the cell. The glycosylation of the amyloid is altered in the brain of an Alzheimer’s patient, research suggests. Therefore, the protein is being processed in such a way where more beta-amyloid is being produced. This mutation no matter how small, can play a huge role in how the protein functions. Proteins have a unique shape determined by the interactions of their side chains. The shape the protein forms usually has to match with another molecule or structure. If the structure is mutated in any way, the protein may not remain the same shape and therefore not match the shape of another molecule or structure. This causes a change in the function. Therefore in this case with amyloid, how the protein is glycosylated will determine where it ends up in the cell membrane, due to shape and this will determine if an enzyme will break it down or not.
The research found a difference between Alzheimer and non-alzheimer patients in terms of how APP is glycosylated. The patterns of APP glycosylation were evidently different. The patterns of proteins are so crucial to their function and structure. So, researchers were able to perform a chemical analysis and found that these different patterns may be a result of different processing of the protein. By processing APP differently, it may trigger Alzheimers. The protein structure is changed and the protein will not act the same. Therefore, with this knowledge, by looking for APP that has an altered way of being glycosylated, it may be easier to detect Alzheimers and inspire treatments in the future. This research is so exciting and important because one day it can help with Alzheimer’s treatments. Not only will it be a great detection test, but the by preventing the creation of beta-amyloid Alzheimers may be preventable in the future or easier to spot. Do you think this sounds like a promising next step to Alzheimer’s detection and treatment?
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