Islet amyloid polypeptide toxicity and membrane interactions

Cao, Ping; Abedini, Andisheh; Wang, Hui; Tu, Ling-Hsien; Zhang, Xiaoxue; Schmidt, Ann Marie; Raleigh, Daniel P.

doi:10.1073/pnas.1305517110

Cited by 146Alzheimer's disease research and treatmentsPancreatic function and diabetesLipid Membrane Structure and Behavior

Islet amyloid polypeptide toxicity and membrane interactions

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Cao, Ping, Abedini, Andisheh, Wang, Hui, Tu, Ling-Hsien, Zhang, Xiaoxue, Schmidt, Ann Marie, Raleigh, Daniel P.·2013·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1305517110PMC PMC3845181

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Abstract

Significance: Amyloid formation is a hallmark of a range of human diseases. The polypeptide hormone amylin forms amyloid deposits in type 2 diabetes, and amyloid formation is thought to be a contributor to the decline in β-cell mass in the disease, however the basis of amylin-induced cytotoxicity is not fully understood. Amylin-induced membrane disruption has attracted considerable interest, and the interactions of amylin with model membranes have been characterized, but the relationship between studies with model membranes and toxicity is not understood. In this article the relationship between cell toxicity and the ability to disrupt model membranes is examined. There is no direct correlation between the two processes.

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Recent transplantation results suggest amylin oligomers play a key role in progressive beta cell failure.
“Recent results from transplantation of human and transgenic animal islets suggest that oligomers of amylin play a key role in the progressive failure of ␤ cells (25,216).”
From The Activity of Peptides of the Calcitonin Family in Bone (2019) · cites this paper as [25]
The paper’s introductory section says IAPP amyloid formation contributes to islet-transplant failure and that islet amyloid contributes to declining β-cell mass. It does not specifically attribute progressive β-cell failure to amylin oligomers on the basis of transplantation results from both human and transgenic animal islets. No page number is available in our copy. (LLM, conf=0.87)
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Authors: Cao, P., Abedini, A., Wang, H., Tu, L.-H., Zhang, X., Schmidt, A. M., & Raleigh, D. P.
Affiliations: Stony Brook University (US)
NYU Langone Health (US)
ORCID: Cao, Ping
Abedini, Andisheh
Wang, Hui
Tu, Ling-Hsien
Zhang, Xiaoxue
Schmidt, Ann Marie
Raleigh, Daniel P.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2013-11-11
Volume: 110
Issue: 48
Pages: 19279-19284
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1305517110
PMC: PMC3845181
OpenAlex: W1980138515
Cited by: 146
References: 48
Citations by year: 2026: 5 · 2025: 6 · 2024: 6 · 2023: 10 · 2022: 7 · 2021: 5 · 2020: 15 · 2019: 13 · 2018: 26 · 2017: 16 · 2016: 6 · 2015: 21 · 2014: 9 · 2013: 1
FWCI: 8.56
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM078114, R01GM078114)
National Institute of Diabetes and Digestive and Kidney Diseases (F32DK089734)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords: amylin, membrane leakage, amyloid fibril formation, type 2 diabetes, islet transplantation, fibril growth, lipid rafts, cholesterol, pramlintide, cytotoxicity
MeSH terms: Amino Acid Sequence, Amyloid, Animals, Biophysics, Diabetes Mellitus, Type 2, Humans, Membranes, Artificial, Molecular Sequence Data, Oxazines, Species Specificity, Thiazoles, Xanthenes, Microscopy, Electron, Transmission, Rats, Benzothiazoles, Islet Amyloid Polypeptide

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Islet amyloid polypeptide toxicity and membrane interactions

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