Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes.
Abstract
Islet amyloid has been recognized as a pathological entity in type 2 diabetes since the turn of the century. It has as its unique component the islet beta-cell peptide islet amyloid polypeptide (IAPP), or amylin, which is cosecreted with insulin. In addition to this unique component, islet amyloid contains other proteins, such as apolipoprotein E and the heparan sulfate proteoglycan perlecan, which are typically observed in other forms of generalized and localized amyloid. Islet amyloid is observed at pathological examination in the vast majority of individuals with type 2 diabetes but is rarely observed in humans without disturbances of glucose metabolism. In contrast to IAPP from rodents, human IAPP has been shown to form amyloid fibrils in vitro. Because all human subjects produce and secrete the amyloidogenic form of IAPP, yet not all develop islet amyloid, some other factor(s) must be involved in islet amyloid formation. One hypothesis is that an alteration in beta-cell function resulting in a change in the production, processing, and/or secretion of IAPP is critical to the initial formation of islet amyloid fibrils in human diabetes. This nidus of amyloid fibrils then allows the progressive accumulation of IAPP-containing fibrils and the eventual replacement of beta-cell mass by amyloid and contributes to the development of hyperglycemia. One factor that may be involved in producing the changes in the beta-cell that result in the initiation of amyloid formation is the consumption of increased dietary fat. Dietary fat is known to alter islet beta-cell peptide production, processing, and secretion, and studies in transgenic mice expressing human IAPP support the operation of this mechanism. Further investigation using this and other models should provide insight into the mechanism(s) involved in islet amyloidogenesis and allow the development of therapeutic agents that inhibit or reverse amyloid fibril formation, with the goal being to preserve beta-cell function and improve glucose control in type 2 diabetes.
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Islet amyloid deposition is found in up to 90% of patients with Type 2 diabetes.
“One factor that we and others have been examining is the deposition of amyloid, which is found in the islets of up to 90% of patients with Type 2 diabetes [128, 129].”
From The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes (2003) · cites this paper as [129]
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- Authors
- Kahn, S. E., Andrikopoulos, S., & Verchere, C. B.
- Affiliations
- University of Washington (US)
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 1999-02-01
- Volume
- 48
- Issue
- 2
- Pages
- 241-253
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W1992231742
- Cited by
- 488
- References
- 0
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 9 · 2023: 10 · 2022: 16 · 2021: 11 · 2020: 15 · 2019: 13 · 2018: 24 · 2017: 12 · 2016: 18 · 2015: 17 · 2014: 21 · 2013: 17 · 2012: 25
- FWCI
- 24.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK050703, DK48152, DK50703, R01DK048152, DK-17047, P30DK017047)
- Topics
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Keywords
- islet amyloid, type 2 diabetes, amylin, beta-cell function, amyloid fibril formation, apolipoprotein E, perlecan, dietary fat, hyperglycemia, beta-cell mass loss, amyloidogenesis
- MeSH terms
- Amyloid, Amyloidosis, Animals, Diabetes Mellitus, Type 2, Dietary Fats, Humans, Islets of Langerhans, Islet Amyloid Polypeptide
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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