Misfolded and damaged proteins are common to all human neurodegenerative diseases. Clumps of these aggregated proteins destroy neurons within the brain and cause disease. But explanations for the mechanism that actually causes cell death have varied widely, puzzling scientists and leading them to ask whether Alzheimers, Parkinsons, Huntingtons and Creutzfeldt-Jakob diseases and familial amyotrophic lateral sclerosis (ALS) are related diseases or very different diseases.
Northwestern University scientists now offer a clue that may get to the core of the cell death question and establish a common mechanism in these diseases. In a study to be published online Feb. 9 by the journal Science, the research team shows that polyglutamine (the toxic component of the protein responsible for Huntingtons disease) is so demanding on the cells system that it changes the environment within the cell, causing other metastable, or partially folded, proteins to crash and lose function. Over time, this can cause the organism to die.
"Our results suggest that these disease-associated, aggregation-prone proteins may exert their destabilizing effects by interfering generally with other proteins that are having difficulty folding," said Richard I. Morimoto, Bill and Gayle Cook Professor of Biochemistry, Molecular Biology and Cell Biology, who led the study. Morimoto is an expert in Huntingtons disease and on the cellular and molecular response to damaged proteins.
Megan Fellman | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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