A decade of research links misfolded proteins to Alzheimer's and diabetes
In short: A review of research from the past decade describes how normally functional proteins can misfold and clump into amyloid aggregates that are hard for cells to break down. This process has been linked to a growing list of human disorders, including Alzheimer's and Parkinson's diseases, type II diabetes, and various systemic amyloidoses.
The review catalogs which proteins misfold into amyloid in human tissues, the diseases linked to them, and genetic clues about how these diseases begin, alongside newer findings on amyloid fibril structure and a cellular network that normally guards against protein misfolding.
As a review of existing research rather than new experiments, it doesn't test treatments directly, and the authors note that these disorders still lack therapies that address the misfolding process itself.
Why it matters: A shared biological process, protein misfolding into amyloid, connects seemingly different diseases from Alzheimer's to diabetes.
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Sources
- Source: Research: Chiti and Dobson (2017). Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annual Review of Biochemistry. · other-oa
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