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Amyloid in the islets of Langerhans: Thoughts and some historical aspects
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Immunology, Genetics and Pathology, Molecular and Morphological Pathology.
2011 (English)In: Upsala Journal of Medical Sciences, ISSN 0300-9734, E-ISSN 2000-1967, Vol. 116, no 2, 81-89 p.Article, review/survey (Refereed) Published
Abstract [en]

Deposition of amyloid, derived from the polypeptide hormone islet amyloid polypeptide (IAPP; 'amylin') is the single most typical islet alteration in type 2 diabetes. Islet amyloid was described as hyalinization already in 1901, but not until 1986 was it understood that it is a polymerization product of a novel beta-cell regulatory product. The subject of this focused review deals with the pathogenesis and importance of the islet amyloid itself, not with the biological effect of the polypeptide. Similar to the situation in Alzheimer's disease, it has been argued that the amyloid may not be of importance since there is no strict correlation between the degree of islet amyloid infiltration and the disease. However, it is hardly discussable that the amyloid is important in subjects where islets have been destroyed by pronounced islet amyloid deposits. Even when there is less islet amyloid the deposits are widely spread, and beta-cells show ultrastructural signs of cell membrane destruction. It is suggested that type 2 diabetes is heterogeneous and that in one major subtype aggregation of IAPP into amyloid fibrils is determining the progressive loss of beta-cells. Interestingly, development of islet amyloid may be an important event in the loss of beta-cell function after islet transplantation into type 1 diabetic subjects.

Place, publisher, year, edition, pages
2011. Vol. 116, no 2, 81-89 p.
Keyword [en]
Amyloid, beta-cell mass, beta-cells, IAPP, islets of Langerhans, protein aggregation, type 2 diabetes
National Category
Clinical Laboratory Medicine
URN: urn:nbn:se:uu:diva-152803DOI: 10.3109/03009734.2011.573884ISI: 000289467100001PubMedID: 21486192OAI: oai:DiVA.org:uu-152803DiVA: diva2:414472
Available from: 2011-05-03 Created: 2011-05-02 Last updated: 2014-08-15Bibliographically approved

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