Journal
CURRENT OPINION IN PHARMACOLOGY
Volume 43, Issue -, Pages 104-110Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.coph.2018.08.016
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Funding
- 'Institut National de la Sante et de la Recherche Medicale' (INSERM, Paris, France)
- 'Societe Francophone du Diabete' (SFD, Paris, France)
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The islet in type 2 diabetes is characterized by beta-cell dysfunction and deficit, increased beta-cell apoptosis and amyloid deposits that derived from islet amyloid polypeptide (IAPP). In species such as humans that are vulnerable to developing type 2 diabetes, IAPP has the propensity to form toxic oligomers that contribute to beta-cell dysfunction and apoptosis, defining type 2 diabetes as a protein misfolding disorder. In this report, we review mechanisms known to contribute to protein misfolding and formation of toxic oligomers, and the deleterious consequences of these oligomers on beta-cell function and survival. Finally, we will consider approaches to prevent protein misfolding and formation of toxic oligomers as potential novel therapeutic targets for type 2 diabetes and other protein misfolding diseases.
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