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- W2951374313 abstract "Abstract The islet in type 2 diabetes (T2D) is characterized by amyloid deposits derived from islet amyloid polypeptide (IAPP), a protein co-expressed with insulin by β-cells. In common with amyloidogenic proteins implicated in neurodegeneration, human IAPP (hIAPP) forms membrane permeant toxic oligomers implicated in misfolded protein stress. Here, we establish that hIAPP misfolded protein stress activates HIF1α/PFKFB3 signaling, this increases glycolysis disengaged from oxidative phosphorylation with mitochondrial fragmentation and perinuclear clustering, considered a protective posture against increased cytosolic Ca 2+ characteristic of toxic oligomer stress. In contrast to tissues with the capacity to regenerate, β-cells in adult humans are minimally replicative, and therefore fail to execute the second pro-regenerative phase of the HIF1α/PFKFB3 injury pathway. Instead, β-cells in T2D remain trapped in the pro-survival first phase of the HIF1α injury repair response with metabolism and the mitochondrial network adapted to slow the rate of cell attrition at the expense of β-cell function." @default.
- W2951374313 created "2019-06-27" @default.
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- W2951374313 date "2019-06-18" @default.
- W2951374313 modified "2023-10-14" @default.
- W2951374313 title "IAPP toxicity activates HIF1α/PFKFB3 signaling delaying β-cell loss at the expense of β-cell function" @default.
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- W2951374313 doi "https://doi.org/10.1038/s41467-019-10444-1" @default.
- W2951374313 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6581914" @default.
- W2951374313 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31213603" @default.