The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species
Abstract
Amyloid deposits in the islets of Langerhans occur in association with type 2 diabetes mellitus (DM) in humans and cats and consist of a 37‐amino‐acid polypeptide known as islet amyloid polypeptide (IAPP). In order to find an explanation for the situation that islet amyloid (IA) does not develop in common rodent species, we have deduced the amino acid sequence of the IAPP molecule in mouse, rat and hamster. We find that a specific region of the molecule diverges to a high degree. Synthetic peptides corresponding to this region of human and hamster IAPP were compared for their ability to form amyloid fibrils in vitro. Whereas the human peptide readily formed fibrils with amyloid character, the hamster peptide completely lacked this property. We suggest this to be a likely explanation for the differences in IA formation between humans and rodents and discuss our findings in relation to the type 2 DM syndrome.
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Cites
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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.84.23.8628 · Cited by 1,299
Abnormal patterns of insulin secretion in non-insulin-dependent diabetes mellitus.
Polonsky, K. S., Given, B. D., Hirsch, L. J., Tillil, H., Shapiro, E. T., Beebe, C., Frank, B. H., Galloway, J. A., & Van Cauter, E. (1988) · New England Journal of Medicine · doi:10.1056/nejm198805123181903 · Cited by 567
Cited by
Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044
Self-citationIncreased Risk of Type 2 Diabetes in Alzheimer Disease
Janson, J., Laedtke, T., Parisi, J. E., O’Brien, P., Petersen, R. C., & Butler, P. C. (2004) · Diabetes · doi:10.2337/diabetes.53.2.474 · Cited by 950
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
Westermark, P., Engström, U., Johnson, K. H., Westermark, G. T., & Betsholtz, C. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5036 · Cited by 807
Self-citationSpontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide.
Janson, J., Soeller, W. C., Roche, P. C., Nelson, R. T., Torchia, A. J., Kreutter, D. K., & Butler, P. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.14.7283 · Cited by 342
Zhao, W.-Q., & Townsend, M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.10.014 · Cited by 291
Metadata
- Authors
- Betsholtz, C., Christmansson, L., Engström, U., Rorsman, F., Svensson, V., Johnson, K. H., & Westermark, P.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1989-07-17
- Volume
- 251
- Issue
- 1-2
- Pages
- 261-264
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2082592680
- Cited by
- 176
- References
- 3
- FWCI
- 8.90
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. https://app.cochat.ai/papers/10.1016/0014-5793(89)81467-x
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- Betsholtz, C., Christmansson, L., Engström, U., Rorsman, F., Svensson, V., Johnson, K. H., & Westermark, P. (1989). Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. FEBS Letters. https://doi.org/10.1016/0014-5793(89)81467-x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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