Impaired processing of human pro-islet amyloid polypeptide is not a causative factor for fibril formation or membrane damage in vitro
Biochemistry, ISSN: 0006-2960, Vol: 48, Issue: 46, Page: 10918-10925
2009
- 22Citations
- 40Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations22
- Citation Indexes22
- 22
- CrossRef19
- Captures40
- Readers40
- 40
Article Description
Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus (DM2). hIAPP is synthesized by islet β-cells initially as a preprohormone, processing of which occurs in several steps. It has been suggested that in DM2 this processing is defective and that aggregation of the processing intermediates prohIAPP and prohIAPP may represent the initial step in formation of islet amyloid. Here we investigate this possibility by analyzing the aggregation, the structure, and the membrane interaction of mature hIAPP and its precursors, prohIAPP and prohIAPP, in vitro. Our data reveal that both precursors form amyloid fibrils in solution but not in the presence of membranes. This inhibition is in contrast to the catalyzing effect of membranes on fibril formation of mature hIAPP. Importantly, in the presence of membranes, both precursors are able to inhibit fibrillogenesis of mature hIAPP. These differences in behavior between mature hIAPP and its precursors are most likely related to differences in their mode of membrane insertion. Both precursors insert efficiently and adopt an α-helical structure even with a high lipid/peptide ratio, while mature hIAPP rapidly adopts a β-sheet conformation. Furthermore, while mature hIAPP affects the barrier properties of lipid vesicles, neither of the precursors is able to induce membrane leakage. Our study suggests that the hIAPP precursors prohIAPP and prohIAPP do not serve as amyloid initiators but rather prevent aggregation and membrane damage of mature hIAPP in early stages of its biosynthesis and intracellular transport. © 2009 American Chemical Society.
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