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Saturday, April 12, 2014

Shape-shifting disease proteins may explain variable appearance of neurodegenerative diseases


Altered protein shapes may explain differences in some brain diseases
Accumulations of alpha-synuclein (red) and tau (green) were found in mouse brain cells that had been treated with strain B. Overlap of the two proteins is shown in yellow. Credit: Courtesy of Dr. Virginia M.Y. Lee, University of Pennsylvania School of Medicine.
Neurodegenerative diseases are not all alike. Two individuals suffering from the same disease may experience very different age of onset, symptoms, severity, and constellation of impairments, as well as different rates of disease progression. Researchers in the Perelman School of Medicine at the University of Pennsylvania have shown one disease protein can morph into different strains and promote misfolding of other disease proteins commonly found in Alzheimer's, Parkinson's and other related neurodegenerative diseases.
Virginia M.Y. Lee, PhD, MBA, professor of Pathology and Laboratory Medicine and director of the Center for Neurodegenerative Disease Research, with co-director, John Q. Trojanowski MD, PhD, postdoctoral fellow Jing L. Guo, PhD, and colleagues, discovered that alpha-synuclein, a protein that forms sticky clumps in the neurons of Parkinson's disease patients, can exist in at least two different structural shapes, or "strains," when it clumps into fibrils, despite having precisely the same.
These two strains differ in their ability to promote fibril formation of normal alpha-synuclein, as well as the , which forms neurofibrillary tangles in individuals with Alzheimer's disease.
Importantly, these alpha-synuclein strains are not static; they somehow evolve, such that fibrils that initially cannot promote tau tangles acquire that ability after multiple rounds of "seeded" fibril formation in test tubes.
The findings appear in the July 3rd issue of Cell.
Morphed Misfolding Proteins Found In Overlapping Neurodegenerative Diseases
Tau and alpha-synuclein protein  are hallmarks of separate diseases – Alzheimer's and Parkinson's, respectively. Yet these two proteins are often found entangled in diseased brains of patients who may manifest symptoms of both disorders.
One possible explanation for this convergence of Alzheimer's and Parkinson's  in the same patient is a global disruption in . But, Guo and Lee showed that one strain of alpha-synuclein  which cannot promote tau fibrillization actually evolved into another strain that could efficiently cause tau to fibrillize in cultured neurons, although both strains are identical at the amino acid sequence level. Guo and Lee called the starting conformation "Strain A," and the evolved conformation, "Strain B."

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