ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2012
Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 80 citations in OpenAlex.
- Prion Protein-Derived Cell-Penetrating Peptide Inhibits Type II Diabetes-Associated Islet Amyloid Polypeptide Aggregation and Cytotoxicity.Biochemistry · 2026Article
- Coenzyme Q10 Enhances Resilience of Mitochondrial-like Membranes Against Amyloidogenic Peptides.Membranes · 2025Article
- The Effect of Calcium Ions on hIAPP Channel Activity: Possible Implications in T2DM.Membranes · 2023Article
- Contribution of the 12-17 hydrophobic region of islet amyloid polypeptide in self-assembly and cytotoxicity.Frontiers in molecular biosciences · 2022Article
- FoxA2 and RNA Pol II mediate human islet amyloid polypeptide turnover in ER-stressed pancreatic β-cells.The Biochemical journal · 2021Article
- Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins.ACS chemical neuroscience · 2020Article
- Are Heat Shock Proteins an Important Link between Type 2 Diabetes and Alzheimer Disease?International journal of molecular sciences · 2020Review
- Tryptophan-galactosylamine conjugates inhibit and disaggregate amyloid fibrils of Aβ42 and hIAPP peptides while reducing their toxicity.Communications biology · 2020Article
- Supercritical COACS omega · 2020Article
- Aggregation of biologically important peptides and proteins: inhibition or acceleration depending on protein and metal ion concentrations.RSC advances · 2019Review
- Apoptosis signal regulating kinase-1 and NADPH oxidase mediate human amylin evoked redox stress and apoptosis in pancreatic beta-cells.Biochimica et biophysica acta. Biomembranes · 2018Article
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- A Rationally Designed Hsp70 Variant Rescues the Aggregation-Associated Toxicity of Human IAPP in Cultured Pancreatic Islet β-Cells.International journal of molecular sciences · 2018Article
- Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid.Nature communications · 2018Article
- Active Immunization Against hIAPP Oligomers Ameliorates the Diabetes- Associated Phenotype in a Transgenic Mice Model.Scientific reports · 2017Article
- Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017Review
- Amylin alters human brain pericyte viability and NG2 expression.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2017Article
- Article
- C4b-binding Protein Protects β-Cells from Islet Amyloid Polypeptide-induced Cytotoxicity.The Journal of biological chemistry · 2016Article
- Proteasome regulates turnover of toxic human amylin in pancreatic cells.The Biochemical journal · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Islet amyloid polypeptide (IAPP) is a peptide hormone cosecreted with insulin by pancreatic β-cells. In type II diabetes, IAPP aggregates in a process that is associated with β-cell dysfunction and loss of β-cell mass. The relationship between IAPP's conformational landscape and its capacity to mediate cell death remains poorly understood. We have addressed these unknowns by comparing the cytotoxic effects of sequence variants with differing α-helical and amyloid propensities. IAPP was previously shown to oligomerize cooperatively on binding to lipid bilayers. Here, comparable transitions are evident in cell culture and are associated with a change in subcellular localization to the mitochondria under toxic conditions. Notably, we find that this toxic gain of function maps to IAPP's capacity to adopt aggregated membrane-bound α-helical, and not β-sheet, states. Our findings suggest that upon α-helical mediated oligomerization, IAPP acquires cell-penetrating peptide (CPP) properties, facilitating access to the mitochondrial compartment, resulting in its dysfunction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.