ArticleScientific reports2017
Novel insight into streptozotocin-induced diabetic rats from the protein misfolding perspective.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers, 2 of them syntheses that pooled it.
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Who cites it
9 citing papers in PubMed, 2 syntheses or guidelines pooled it, 16 citations in OpenAlex.
- Decoding the Contribution of IAPP Amyloid Aggregation to Beta Cell Dysfunction: A Systematic Review and Epistemic Meta-Analysis of Type 1 Diabetes.International journal of molecular sciences · 2025Pooled it
- Amyloid Biomarkers in Conformational Diseases at Face Value: A Systematic Review.Molecules (Basel, Switzerland) · 2017Pooled it
- Therapeutic Potential of Holothuria leucospilota Extract in STZ-Induced Diabetic Rats: Targeting Inflammation and Apoptosis at the Gene Expression Level.Endocrinology, diabetes & metabolism · 2026Article
- The Link between Type 2 Diabetes Mellitus and the Polymorphisms of Glutathione-Metabolizing Genes Suggests a New Hypothesis Explaining Disease Initiation and Progression.Life (Basel, Switzerland) · 2021Article
- Oxygen Generating Polymeric Nano Fibers That Stimulate Angiogenesis and Show Efficient Wound Healing in a Diabetic Wound Model.International journal of nanomedicine · 2020Article
- Observational
- 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
- Comparative Effect Of Curcumin Versus Liposomal Curcumin On Systemic Pro-Inflammatory Cytokines Profile, MCP-1 And RANTES In Experimental Diabetes Mellitus.International journal of nanomedicine · 2019Article
- Diabetes Drug Discovery: hIAPPMolecules (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein folding is a process of self-assembly defined by the sequence of the amino acids of the protein involved. Additionally, proteins tend to unfold, misfold and aggregate due to both intrinsic and extrinsic causes. Human islet amyloid polypeptide (hIAPP) aggregation is an early step in diabetes mellitus. However, the aggregation of rat IAPP (rIAPP) remains an open question. Adult female Sprague-Dawley rats weighing 150-250 g were divided into two groups. The experimental group (streptozotocin [STZ]) (n = 21) received an intraperitoneal injection of a single dose of 40 mg/kg STZ. We used the mouse anti-IAPP antibody and the anti-amyloid oligomer antibody to study the temporal course of rIAPP oligomerization during STZ-induced diabetes using a wide array of methods, strategies and ideas derived from biochemistry, cell biology, and proteomic medicine. Here, we demonstrated the tendency of rIAPP to aggregate and trigger cooperative processes of self-association or hetero-assembly that lead to the formation of amyloid oligomers (trimers and hexamers). Our results are the first to demonstrate the role of rIAPP amyloid oligomers in the development of STZ-induced diabetes in rats. The IAPP amyloid oligomers are biomarkers of the onset and progression of diabetes and could play a role as therapeutic targets.
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Registered trials
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