| RRC ID |
77860
|
| 著者 |
Suginoma H, Owada R, Katano-Toki A, Mori A, Fujioka J, Nakamura K.
|
| タイトル |
Non-fibril form but not fibril form of human islet amyloid polypeptide 8-20 changes brain functions in mice.
|
| ジャーナル |
PLoS One
|
| 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.
|
| 巻・号 |
19(1)
|
| ページ |
e0296750
|
| 公開日 |
2024-1-1
|
| DOI |
10.1371/journal.pone.0296750
|
| PII |
PONE-D-23-10509
|
| PMID |
38181010
|
| PMC |
PMC10769099
|
| MeSH |
Animals
Brain
Cytoskeleton
Humans
Islet Amyloid Polypeptide
Mice
Nervous System Physiological Phenomena*
Peptide Hormones*
|
| IF |
2.74
|
| リソース情報 |
| ヒト・動物細胞 |
PC-12(RCB0009) |
