Cited by 807Alzheimer's disease research and treatmentsPancreatic function and diabetesPrion Diseases and Protein Misfolding

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Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.

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Westermark, P, Engström, U, Johnson, K H, Westermark, G T, Betsholtz, C·1990·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.87.13.5036PMC PMC54256

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Abstract

Islet amyloid polypeptide (IAPP), a putative polypeptide hormone, is a product of pancreatic beta-cells and the major constituent of the amyloid deposits seen mainly in islets of type 2 diabetic humans and diabetic cats. The connection between IAPP amyloid formation and diabetes is unknown, but a limited segment of the IAPP molecule, positions 20-29, seems responsible for the aggregation to fibrils. Differences in the amino acid sequence of this region probably determine whether or not islet amyloid can develop in a particular species. Amyloid fibril formation can be mimicked in vitro with the aid of synthetic peptides. With this technique we show that peptides corresponding to IAPP positions 20-29 of human and cat, species that develop IAPP-derived islet amyloid, form amyloid-like fibrils in vitro. The corresponding IAPP segment from three rodent species that do not develop IAPP-derived amyloid did not give rise to fibrils. Substitution of the human IAPP-(20-29) decapeptide with one or two amino acid residues from species without islet amyloid generally reduced the capacity to form fibrils. We conclude that the sequence Ala-Ile-Leu-Ser-Ser, corresponding to positions 25-29 of human IAPP, is strongly amyloidogenic and that a proline-for-serine substitution in position 28, as in several rodents, almost completely inhibits formation of amyloid fibrils.

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Self-citation
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Authors: Westermark, P., Engström, U., Johnson, K. H., Westermark, G. T., & Betsholtz, C.
Affiliations: Linköping University Hospital (SE)
ORCID: Westermark, P
Westermark, G T
Betsholtz, C
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1990-07
Volume: 87
Issue: 13
Pages: 5036-5040
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.87.13.5036
PMC: PMC54256
OpenAlex: W2061111679
Cited by: 807
References: 30
Citations by year: 2026: 18 · 2025: 20 · 2024: 27 · 2023: 17 · 2022: 25 · 2021: 31 · 2020: 43 · 2019: 21 · 2018: 28 · 2017: 41 · 2016: 36 · 2015: 36 · 2014: 29 · 2013: 33 · 2012: 36
FWCI: 7.26
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)
Funders: National Institutes of Health (5r01dk036734-06)
Medical Research Council
National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK36734)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Keywords: amylin, amyloid fibril formation, type 2 diabetes, pancreatic beta cells, peptide aggregation
MeSH terms: Amino Acid Sequence, Amyloid, Amyloidosis, Animals, Cats, Diabetes Mellitus, Type 2, Cricetinae, Humans, Islets of Langerhans, Microscopy, Electron, Molecular Sequence Data, Mutation, Protein Precursors, Sequence Homology, Nucleic Acid, Species Specificity, Rats, Islet Amyloid Polypeptide

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Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.

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