The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.
Open accessAbstract
Deposition of amyloid in pancreatic islets is a common feature in human type 2 diabetic subjects but because of its insolubility and low tissue concentrations, the structure of its monomer has not been determined. We describe a peptide, of calculated molecular mass 3905 Da, that was a major protein component of amyloid-rich pancreatic extracts of three type 2 diabetic patients. After collagenase treatment, an extract containing 20-50% amyloid was solubilized by sonication into 70% formic acid and the peptide was purified by gel filtration followed by reverse-phase high-performance liquid chromatography. We term this peptide diabetes-associated peptide, as it was not detected in extracts of pancreas from any of six normal subjects. Diabetes-associated peptide contains 37 amino acids and is 46% identical to the sequences of rat and human calcitonin gene-related peptide, indicating that these peptides are related in evolution. Sequence identities with conserved residues of the insulin A chain were also seen in a 16-residue segment. On extraction, the islet amyloid is particulate and insoluble like the core particles of Alzheimer disease. Their monomers have similar molecular masses, each having a hydropathic region that can probably form beta-pleated sheets. The accumulation of amyloid, including diabetes-associated peptide, in islets may impair islet function in type 2 diabetes mellitus.
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“These deposits contain IAPP as their unique peptide component [130, 131].”
From The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes (2003) · cites this paper as [131]
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Metadata
- Authors
- Cooper, G. J., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., & Reid, K. B.
- Affiliations
- University of Oxford (GB)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1987-12
- Volume
- 84
- Issue
- 23
- Pages
- 8628-8632
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC299599
- OpenAlex
- W2067820229
- Cited by
- 1,299
- References
- 38
- Citations by year
- 2026: 23 · 2025: 26 · 2024: 16 · 2023: 29 · 2022: 30 · 2021: 42 · 2020: 45 · 2019: 39 · 2018: 47 · 2017: 49 · 2016: 26 · 2015: 34 · 2014: 35 · 2013: 48 · 2012: 42
- FWCI
- 42.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (submittedVersion)
- 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 › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
- Keywords
- islet amyloid, type 2 diabetes, pancreatic islets, calcitonin gene-related peptide, insulin A chain, islet dysfunction
- MeSH terms
- Aged, Amino Acid Sequence, Amino Acids, Amyloid, Diabetes Mellitus, Type 2, Humans, Insulin, Islets of Langerhans, Molecular Sequence Data, Neuropeptides, Calcitonin Gene-Related Peptide, Islet Amyloid Polypeptide
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