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Reciprocal Molecular Interactions between the A beta Peptide Linked to Alzheimer's Disease and Insulin Linked to Diabetes Mellitus Type II
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 4
2016 (English)In: ACS Chemical Neuroscience, ISSN 1948-7193, E-ISSN 1948-7193, Vol. 7, no 3, 269-274 p.Article in journal (Refereed) Published
Abstract [en]

Clinical studies indicate diabetes mellitus type II (DM) doubles the risk that a patient will also develop Alzheimer's disease (AD). DM is caused by insulin resistance and a relative lack of active insulin. AD is characterized by the deposition of amyloid beta (A beta) peptide fibrils. Prior to fibrillating, A beta forms intermediate, prefibrillar oligomers, which are more cytotoxic than the mature A beta fibrils. Insulin can also form amyloid fibrils. In vivo studies have revealed that insulin promotes the production of A beta, and that soluble A beta competes with insulin for the insulin receptor. Here, we report that monomeric insulin interacted with soluble A beta and that both molecules reciprocally slowed down the aggregation kinetics of the other. Prefibrillar oligomers of A beta that eventually formed in the presence of insulin were less cytotoxic than A beta oligomers formed in the absence of insulin. Mature A beta fibrils induced fibrillation of soluble insulin, but insulin aggregates did not promote A beta fibrillation. Our study indicates that direct molecular interactions between insulin and A beta may contribute to the strong link between DM and AD.

Place, publisher, year, edition, pages
2016. Vol. 7, no 3, 269-274 p.
Keyword [en]
Amyloid beta peptides, Alzheimer's disease, insulin, diabetes mellitus type II, cross amyloid interaction, fibrillation
National Category
Biological Sciences Neurosciences
URN: urn:nbn:se:su:diva-129624DOI: 10.1021/acschemneuro.5b00325ISI: 000372479600002PubMedID: 26785771OAI: diva2:925553
Available from: 2016-05-02 Created: 2016-04-26 Last updated: 2016-05-02Bibliographically approved

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Wärmländer, Sebastian K. T. S.Gräslund, Astrid
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