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- Title
Non-fibril form but not fibril form of human islet amyloid polypeptide 8–20 changes brain functions in mice.
- Authors
Suginoma, Hinaho; Owada, Ryuji; Katano-Toki, Akiko; Mori, Ayaka; Fujioka, Jun; Nakamura, Kazuhiro
- Abstract
Whether fibril formation increases or decreases cytotoxicity remains unclear. Aggregation of human islet amyloid polypeptide (hIAPP), a pivotal regulator of glucose homeostasis, impairs the function and viability of pancreatic β cells. Evidence suggests that low-order oligomers of hIAPP are more toxic to β cells than fibril. However, it remains unclear whether non-fibril form of hIAPP specifically alters brain functions. This study produced fibril and non-fibril forms from a single hIAPP 8–20 peptide. The non-fibril form-injected mice showed changes in spontaneous motor activities, preference for location in the open field and social behavior. In contrast, the fibril-injected mice showed no changes in these behavioral tests. In line with the behavioral changes, the non-fibril form led to impaired neurite outgrowth of cultured neuron-like cells and the loss of neurons in the mouse hippocampus. These findings suggest that non-fibril form but not fibril form of hIAPP changes brain functions.
- Subjects
AMYLIN; PEPTIDES; MICE; ANIMAL social behavior; CYTOTOXINS; OLIGOMERS; AMYLOID beta-protein
- Publication
PLoS ONE, 2024, Vol 19, Issue 1, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0296750