ArticleDiabetology international2018
IAPP/amylin and β-cell failure: implication of the risk factors of type 2 diabetes.
Article in Diabetology international, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 50 citations in OpenAlex.
- QBP1 Peptide as a Potential Anti-Amyloidogenic Therapy for Type 2 Diabetes: An In Vitro Study.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Scrotal hernia in a doguera baboon with diabetes mellitus.The Journal of veterinary medical science · 2026Article
- Structural and morphological dynamics of "on-path" and "off-path" oligomers of human islet amyloid polypeptide.Protein science : a publication of the Protein Society · 2026Article
- Disease-disease interactions: molecular links of neurodegenerative diseases with cancer, viral infections, and type 2 diabetes.Translational neurodegeneration · 2025Review
- The role of hydrophobic collapse in cytotoxic and functional amyloid oligomerization.Biophysical journal · 2025Article
- Analyzing Amylin Aggregation Inhibition Through Quantum Dot Fluorescence Imaging.International journal of molecular sciences · 2024Article
- IAPP - oligomerisation levels in plasma of people with type 2 diabetes.Scientific reports · 2024Article
- Emerging and multifaceted potential contributions of polyphenols in the management of type 2 diabetes mellitus.World journal of diabetes · 2024Review
- Lipid rafts and human diseases: why we need to target gangliosides.FEBS open bio · 2023Review
- Regeneration of Pancreatic Beta Cells by Modulation of Molecular Targets Using Plant-Derived Compounds: Pharmacological Mechanisms and Clinical Potential.Current issues in molecular biology · 2023Review
- How do parasitic worms prevent diabetes? An exploration of their influence on macrophage and β-cell crosstalk.Frontiers in endocrinology · 2023Review
- Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus.Journal of pharmaceutical analysis · 2022Review
- Tissue-Specific Methylation Biosignatures for Monitoring Diseases: An In Silico Approach.International journal of molecular sciences · 2022Article
- Islet Inflammation and β Cell Dysfunction in Type 2 Diabetes.Handbook of experimental pharmacology · 2022Review
- Association of a SNP in theDiabetology international · 2022Article
- Targeting pancreatic beta cell death in type 2 diabetes by polyphenols.Frontiers in endocrinology · 2022Review
- Rice Compounds with Impact on Diabetes Control.Foods (Basel, Switzerland) · 2021Review
- Undercover Toxic Ménage à Trois of Amylin, Copper (II) and Metformin in Human Embryonic Kidney Cells.Pharmaceutics · 2021Article
- Nonhuman IAPP Variants Inhibit Human IAPP Aggregation.Protein and peptide letters · 2021Article
- Tyrosine carbon dots inhibit fibrillation and toxicity of the human islet amyloid polypeptide.Nanoscale advances · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In type 2 diabetes (T2D), the most significant pathological change in pancreatic islets is amyloid deposits, of which a major component is islet amyloid polypeptide (IAPP), also called amylin. IAPP is expressed in β-cells and co-secreted with insulin. Together with the inhibitory effects of synthetic human IAPP (hIAPP) on insulin secretion, our studies, using hIAPP transgenic mice, in which glucose-stimulated insulin secretion was moderately reduced without amyloid deposit, and hIAPP gene-transfected β-cell lines, in which insulin secretion was markedly impaired without amyloid, predicted that soluble hIAPP-related molecules would exert cytotoxicity on β-cells. Human IAPP is one of the most aggregation-prone peptides that interact with cell membranes. While it is widely reported that soluble hIAPP oligomers promote cytotoxicity, this is still a hypothesis since the mechanisms are not yet fully defined. Several hIAPP transgenic mouse models did not develop diabetes; however, in models with backgrounds characterized for diabetic phenotypes, β-cell function and glucose tolerance did worsen, compared to those in non-transgenic models with similar backgrounds. Together with these findings, many studies on metabolic and molecular disorders induced by risk factors of T2D suggest that in T2D subjects, toxic IAPP oligomers accumulate in β-cells, impair their function, and reduce mass through disruption of cell membranes, resulting in β-cell failure. IAPP might be central to β-cell failure in T2D. Anti-amyloid aggregation therapeutics will be developed to create treatments with more durable and beneficial effects on β-cell function.
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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.