Researchers at Lund University in Sweden headed by Professor Singerup Linse and Erik Helistrand have recently identified a molecular mechanism behind the crucial step in Alzheimer’s that leads to the death of brain cells.
The neurological disease is associated, as a general statement, with memory loss and changes in personality. The research at Lund helps identify on a molecular level the chemical reactions which cause plaque, a major benchmark in the progression of the disease, to form. Amyloid beta in its soluble form, found naturally within the brain, acts as a building block and turns into plaque called amyloid fibrils, though the exact pathways of these reactions remain unclear. An early section of the process of formation of fibrils is two small protein fragments of amyloid beta coming together within a nucleus of a cell to form a fibril. Lund University’s study suggests that fibrils have a catalytic surface, allowing reactions to happen quicker while touching them, creating new nuclei which in turn aid the proliferation of more fibrils, causing exponential growth in plaque formation. After a small but crucial amount of amyloid fibrils are created, more immediately surface to begin a self-perpetuating process key to understanding Alzheimer’s. These findings dash what was previously believed; that fibrils formed in single nuclei reactions as a uniform process. More profound perhaps than the catalytic surface is the discovery that this aggregation of amyloid fibrils creates toxic oligomers, small groups of proteins. These oligomers have been identified as neurotoxins that play a significant part in cell-death.
It is the hope of Professor Linse that new medicines targeted at shutting down the catalyzation of amyloid fibrils and the resultant neurotoxins can slow or even stop the progression of the disease. For now, it is heartening that ongoing Alzheimer’s research is yielding new information about the degenerative disease and possible ways to fight its progression.
1) S. I. A. Cohen, S. Linse, L. M. Luheshi, E. Hellstrand, D. A. White, L. Rajah, D. E.
Otzen, M. Vendruscolo, C. M. Dobson, T. P. J. Knowles. Proliferation of amyloid- 42
aggregates occurs through a secondary nucleation mechanism. Proceedings of the National
Academy of Sciences, 2013; DOI: 10.1073/pnas.1218402110
2) Lund University (2013, May 29). Molecular chain reaction in Alzheimer’s disease.
ScienceDaily. Retrieved May 30, 2013, from http://www.sciencedaily.com /releases/2013/05/
By: Lauren Horne
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