Cited by 1,299Pancreatic function and diabetesAlzheimer's disease research and treatmentsAmyloidosis: Diagnosis, Treatment, Outcomes

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Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

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Cooper, G J, Willis, A C, Clark, A, Turner, R C, Sim, R B, Reid, K B·1987·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.84.23.8628PMC PMC299599

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Abstract

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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Authors: Cooper, G. J., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., & Reid, K. B.
Affiliations: University of Oxford (GB)
ORCID: Cooper, G J
Clark, A
Sim, R B
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
DOI: 10.1073/pnas.84.23.8628
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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Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

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