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Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology
Open accessAbstract
The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose homeostasis but aggregates to form islet amyloid in type-2 diabetes. Islet amyloid formation contributes to β -cell dysfunction and death in the disease and to the failure of islet transplants. Recent work suggests a role for IAPP aggregation in cardiovascular complications of type-2 diabetes and hints at a possible role in type-1 diabetes. The mechanisms of IAPP amyloid formation in vivo or in vitro are not understood and the mechanisms of IAPP induced β -cell death are not fully defined. Activation of the inflammasome, defects in autophagy, ER stress, generation of reactive oxygen species, membrane disruption, and receptor mediated mechanisms have all been proposed to play a role. Open questions in the field include the relative importance of the various mechanisms of β -cell death, the relevance of reductionist biophysical studies to the situation in vivo , the molecular mechanism of amyloid formation in vitro and in vivo , the factors which trigger amyloid formation in type-2 diabetes, the potential role of IAPP in type-1 diabetes, the development of clinically relevant inhibitors of islet amyloidosis toxicity, and the design of soluble, bioactive variants of IAPP for use as adjuncts to insulin therapy.
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“It has been demonstrated that amylin analogs, such as pramlintide, dramatically lower body weight, HbA1c levels, and even insulin dosage (98, 99).”
From A critical review on diabetes mellitus type 1 and type 2 management approaches: from lifestyle modification to current and novel targets and therapeutic agents. (2024) · cites this paper as [99]
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“Compared to insulin monotherapy, patients with T1DM who received amylin analog in addition to insulin experienced a greater reduction in pre-prandial hyperglycemia and a corresponding decrease in glucagon levels.”
From A critical review on diabetes mellitus type 1 and type 2 management approaches: from lifestyle modification to current and novel targets and therapeutic agents. (2024) · cites this paper as [99]
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Metadata
- Authors
- Akter, R., Cao, P., Noor, H., Ridgway, Z., Tu, L.-H., Wang, H., Wong, A. G., Zhang, X., Abedini, A., Schmidt, A. M., & Raleigh, D. P.
- Affiliations
- Stony Brook University (US)
- NYU Langone Health (US)
- University College London (GB)
- Corresponding author
- Raleigh, Daniel P.
- ORCID
- Venue
- Journal of Diabetes Research
- Publisher
- Wiley
- Published
- 2016
- Volume
- 2016
- Pages
- 1-18
- ISSN
- 2314-6745 (ISSN-L)
- 2314-6753
- PMC
- PMC4662979
- OpenAlex
- W2209022283
- Cited by
- 273
- References
- 181
- Citations by year
- 2026: 23 · 2025: 33 · 2024: 37 · 2023: 14 · 2022: 26 · 2021: 32 · 2020: 36 · 2019: 21 · 2018: 28 · 2017: 13 · 2016: 10
- FWCI
- 3.26
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Journal of Diabetes Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- National Institutes of Health (GM078114, 5T32GM09271405)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Keywords
- amylin, islet amyloid, type 2 diabetes, beta-cell dysfunction, beta-cell death, islet transplantation, cardiovascular complications, type 1 diabetes, inflammasome, autophagy, endoplasmic reticulum stress, reactive oxygen species, glucose homeostasis
- MeSH terms
- Diabetes Mellitus, Type 2, Humans, Islets of Langerhans, Structure-Activity Relationship, Insulin-Secreting Cells, Islet Amyloid Polypeptide
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