Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.
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Amyloid deposits localized to the islets of Langerhans are typical of non-insulin-dependent human diabetes mellitus and of diabetes mellitus in adult cats. Amyloid deposits also commonly occur in insulin-producing pancreatic tumors. We have purified a major protein--insulinoma or islet amyloid polypeptide (IAPP)--from human and cat islet amyloid and from amyloid of a human insulinoma. IAPP from human insulinoma contained 37 amino acid residues and had a theoretical molecular mass of 3850 Da. The amino acid sequence is unique but has greater than 40% identity with the human calcitonin gene-related peptide. A partial amino acid sequence of cat islet IAPP corresponding to positions 1-27 of human insulinoma IAPP was identical to the human IAPP except for substitutions in three positions. An antiserum raised to a synthetic human insulinoma IAPP-(7-17) undecapeptide showed specific immunohistochemical reactivity with human and cat islet amyloid and with islet B cells. The significance of this pancreatic neuropeptide-like protein is unknown, but it is suggested that it may exert an important endocrine regulatory effect.
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Islet amyloid deposits contain IAPP as their unique peptide component.
“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 [130]
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- Authors
- Westermark, P., Wernstedt, C., Wilander, E., Hayden, D. W., O'Brien, T. D., & Johnson, K. H.
- Affiliations
- Uppsala University (SE)
- University of Minnesota (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1987-06
- Volume
- 84
- Issue
- 11
- Pages
- 3881-3885
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC304980
- OpenAlex
- W2070114315
- Cited by
- 976
- References
- 29
- Citations by year
- 2026: 14 · 2025: 16 · 2024: 14 · 2023: 12 · 2022: 24 · 2021: 23 · 2020: 25 · 2019: 26 · 2018: 35 · 2017: 31 · 2016: 31 · 2015: 26 · 2014: 35 · 2013: 30 · 2012: 35
- FWCI
- 46.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk036734-06)
- Medical Research Council
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK36734)
- Topics
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Health Sciences › Medicine › Epidemiology › Neuroendocrine Tumor Research Advances
- Keywords
- amylin, insulinoma, pancreatic islets, amyloid deposits, type 2 diabetes, calcitonin gene-related peptide, neuropeptides, amino acid sequence, immunohistochemistry, cats, protein purification
- MeSH terms
- Amino Acid Sequence, Amyloid, Animals, Cat Diseases, Cats, Diabetes Mellitus, Diabetes Mellitus, Type 2, Humans, Immunoassay, Insulinoma, Islets of Langerhans, Adenoma, Islet Cell, Pancreatic Neoplasms, Species Specificity
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