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Islet Amyloid Polypeptide (IAPP) Transgenic Rodents as Models for Type 2 Diabetes
Open accessAbstract
Blood glucose concentrations are maintained by insulin secreted from beta-cells located in the islets of Langerhans. There are approximately 2000 beta-cells per islet, and approximately one million islets of Langerhans scattered throughout the pancreas. The islet in type 2 diabetes mellitus (T2D) has deficient beta-cell mass due to increased beta-cell apoptosis and islet amyloid derived from islet amyloid polypeptide (IAPP). Accumulating evidence implicates toxic IAPP oligomers in the mediation of beta-cell apoptosis in T2D. Humans, monkeys, and cats express an amyloidogenic toxic form of IAPP and spontaneously develop diabetes characterized by islet amyloid deposits. However, longitudinal studies of islet pathology in humans are impossible, and studies in nonhuman primates and cats are costly and impractical. Rodent IAPP is not amyloidogenic, thus commonly used rodent models of diabetes do not recapitulate islet pathology in humans. To investigate the diabetogenic role of human IAPP (h-IAPP), several mouse models and, more recently, a rat model transgenic for h-IAPP have been developed. Studies in these models have revealed that the toxic effect of h-IAPP on beta-cell apoptosis demonstrates a threshold-dependent effect. Specifically, increasing h-IAPP transgene expression by breeding or induction of insulin resistance leads to increased beta-cell apoptosis and diabetes. These transgenic rodent models for h-IAPP provide an opportunity to elucidate the mechanisms responsible for h-IAPP-induced beta-cell apoptosis further and to test novel approaches to the prevention and treatment of T2D.
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“The current consensus in the literature is that extracellular plaques of IAPP are not causative of beta-cell pathology, but rather intracellular oligomers of this protein observed in T2D patients (but not in T2D-free individuals) produce the cytotoxic effects.128,131”
From A review of current trends with type 2 diabetes epidemiology, aetiology, pathogenesis, treatments and future perspectives (2021) · cites this paper as [131]
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Metadata
- Authors
- Matveyenko, A. V., & Butler, P. C.
- Affiliations
- University of California, Los Angeles (US)
- Venue
- ILAR Journal
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-01-01
- Volume
- 47
- Issue
- 3
- Pages
- 225-233
- ISSN
- 1084-2020 (ISSN-L)
- OpenAlex
- W2139785451
- Cited by
- 150
- References
- 68
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 8 · 2022: 5 · 2021: 12 · 2020: 7 · 2019: 6 · 2018: 13 · 2017: 9 · 2016: 8 · 2015: 8 · 2014: 7 · 2013: 5 · 2012: 9
- FWCI
- 1.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- ILAR Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Larry L. Hillblom Foundation
- Pfizer
- National Institutes of Health
- University of California, Los Angeles
- U.S. Public Health Service
- National Institute of Diabetes and Digestive and Kidney Diseases (DK59579, R01DK059579)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Diabetes and associated disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Keywords
- amylin, type 2 diabetes, transgenic rodent models, beta-cell apoptosis, beta-cell mass, insulin resistance
- MeSH terms
- Amyloid, Animals, Diabetes Mellitus, Type 2, Disease Models, Animal, Humans, Mice, Transgenic, Insulin-Secreting Cells, Mice, Rats, Islet Amyloid Polypeptide
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