ArticleBiochemistry2014
The ability of insulin to inhibit the formation of amyloid by pro-islet amyloid polypeptide processing intermediates is significantly reduced in the presence of sulfated glycosaminoglycans.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Molecular Mechanisms of Islet Amyloid Polypeptide Aggregation: Towards Chemical Strategies to Prevent Amyloid Formation and to Design Non-Aggregating Peptide Therapeutics.International journal of molecular sciences · 2026Review
- Protein aggregates and biomolecular condensates: implications for human health and disease.Frontiers in molecular biosciences · 2025Review
- Sulfation pathways in the maintenance of functional beta-cell mass and implications for diabetes.Essays in biochemistry · 2024Review
- Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide.Communications biology · 2024Article
- Review
- Substoichiometric Inhibition of Insulin against IAPP Aggregation Is Attenuated by the Incompletely Processed N-Terminus of proIAPP.ACS chemical neuroscience · 2022Article
- Inside the Insulin Secretory Granule.Metabolites · 2021Review
- Elucidating the Relationship Between Diabetes Mellitus and Parkinson's Disease UsingFrontiers in neuroscience · 2020Review
- The Association Between Type 2 Diabetes Mellitus and Parkinson's Disease.Journal of Parkinson's disease · 2020Review
- Unpacking the aggregation-oligomerization-fibrillization process of naturally-occurring hIAPP amyloid oligomers isolated directly from sera of children with obesity or diabetes mellitus.Scientific reports · 2019Article
- The receptor for advanced glycation endproducts is a mediator of toxicity by IAPP and other proteotoxic aggregates: Establishing and exploiting common ground for novel amyloidosis therapies.Protein science : a publication of the Protein Society · 2018Review
- Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson's disease.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Journal of diabetes research · 2016Review
- Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Journal of diabetes research · 2015Review
- Defining the molecular basis of amyloid inhibitors: human islet amyloid polypeptide-insulin interactions.Journal of the American Chemical Society · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Islet amyloid polypeptide (IAPP) is responsible for amyloid deposition in type 2 diabetes and plays an important role in the loss of β-cell mass associated with the disease and in the failure of islet transplants, but the mechanism of islet amyloid formation is not understood. The incorrect processing of proIAPP to produce partially processed forms of the peptide has been proposed to play a role in the initiation of islet amyloid in vivo by promoting interactions with proteoglycans of the extracellular matrix. Insulin is a potent inhibitor of the formation of amyloid by IAPP in vitro in a homogeneous solution; however, its ability to inhibit IAPP in the presence of proteoglycans has not been tested, nor has its effect on the formation of amyloid by proIAPP processing intermediates been examined. Here we show that insulin is a much less effective amyloid inhibitor of both IAPP and proIAPP processing intermediates in vitro in the presence of model glycosaminoglycans, but does inhibit the formation of amyloid by proIAPP processing intermediates in a homogeneous solution. This highlights another mechanism by which sulfated proteoglycans could enhance islet amyloid formation in vivo. Interactions with sulfated proteoglycans can directly promote amyloid formation and can also significantly reduce the effectiveness of natural inhibitors.
Indexed as
Identifiers
What OpenQuestion holds
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.