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Prion-Like Protein Aggregates and Type 2 Diabetes
Abhisek Mukherjee1, Claudio Soto1
1Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Health Science Center, McGovern Medical School, Houston, Texas 77030.
Cold Spring Harbor Perspectives in Medicine
|February 5, 2017
Summary
Misfolded islet amyloid polypeptide (IAPP) aggregates may drive type 2 diabetes (T2D) progression. These aggregates show prion-like transmissibility, similar to other protein misfolding disorders, suggesting a novel mechanism in T2D pathogenesis.
Area of Science:
- Endocrinology
- Molecular Biology
- Neurodegenerative Diseases
Background:
- Type 2 diabetes (T2D) involves insulin resistance and beta-cell dysfunction.
- Accumulation of misfolded islet amyloid polypeptide (IAPP) aggregates in pancreatic islets is implicated in T2D pathogenesis.
- Protein misfolding disorders (PMDs) share amyloid aggregation as a common feature.
Purpose of the Study:
- To review the molecular mechanisms of prion-like transmission of protein aggregates.
- To explore the potential role of this transmission in the development and progression of T2D.
Main Methods:
- Literature review of studies on protein misfolding disorders (PMDs) and T2D.
- Analysis of research on the transmissibility of protein aggregates, including prions.
- Examination of experimental evidence for induced pathology via inoculation of protein aggregates.
Main Results:
- Protein aggregates in PMDs, including Alzheimer's and Parkinson's disease, exhibit transmissibility.
- Misfolded IAPP aggregates in T2D share characteristics with transmissible protein aggregates.
- Experimental models demonstrate that protein aggregates can induce disease hallmarks.
Conclusions:
- The prion-like transmission of protein aggregates is a potential mechanism contributing to pancreatic damage in T2D.
- Understanding this transmission may offer new therapeutic targets for type 2 diabetes.
- Further research is needed to elucidate the precise role of IAPP aggregation and transmission in T2D.
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