Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial Activation
In Alzheimer’s disease, fibrillar amyloid-β (Aβ) peptides form senile plaques associated with microglia. However, the relationship between Aβ peptides and microglia is not fully understood. In this study, the incubation of Aβ1-40 (Aβ40) produced small oligomers, while incubation with Aβ1-42 (Aβ42) c...
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| Format: | Article |
| Language: | English |
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Elsevier
2003-01-01
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| Series: | Journal of Pharmacological Sciences |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1347861319327161 |
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| author | Kazuyuki Takata Yoshihisa Kitamura Masaaki Umeki Daiju Tsuchiya Jun-ichi Kakimura Takashi Taniguchi Peter J. Gebicke-Haerter Shun Shimohama |
| author_facet | Kazuyuki Takata Yoshihisa Kitamura Masaaki Umeki Daiju Tsuchiya Jun-ichi Kakimura Takashi Taniguchi Peter J. Gebicke-Haerter Shun Shimohama |
| author_sort | Kazuyuki Takata |
| collection | DOAJ |
| description | In Alzheimer’s disease, fibrillar amyloid-β (Aβ) peptides form senile plaques associated with microglia. However, the relationship between Aβ peptides and microglia is not fully understood. In this study, the incubation of Aβ1-40 (Aβ40) produced small oligomers, while incubation with Aβ1-42 (Aβ42) caused large molecular aggregates. Microglial production of nitrite, interleukin-6 and tumor necrosis factor-a was induced by Aβ40, but not Aβ42. This production was significantly reduced by 15-deoxy-Δ12,14 prostaglandin J2, and it was completely suppressed by β-sheet breaker peptide, Leu-Pro-Phe-Phe-Asp. These results suggest that small oligomers, rather than large molecular aggregates, mediate microglial activation induced by Aβ peptides. |
| first_indexed | 2024-12-11T09:29:22Z |
| format | Article |
| id | doaj.art-1ff8472ac39a457aa10d2b06f551ca4e |
| institution | Directory Open Access Journal |
| issn | 1347-8613 |
| language | English |
| last_indexed | 2024-12-11T09:29:22Z |
| publishDate | 2003-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Pharmacological Sciences |
| spelling | doaj.art-1ff8472ac39a457aa10d2b06f551ca4e2022-12-22T01:13:02ZengElsevierJournal of Pharmacological Sciences1347-86132003-01-01914330333Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial ActivationKazuyuki Takata0Yoshihisa Kitamura1Masaaki Umeki2Daiju Tsuchiya3Jun-ichi Kakimura4Takashi Taniguchi5Peter J. Gebicke-Haerter6Shun Shimohama7Department of Neurobiology, Kyoto Pharmaceutical University, Kyoto 607-8412, JapanDepartment of Neurobiology, Kyoto Pharmaceutical University, Kyoto 607-8412, JapanDepartment of Neurobiology, Kyoto Pharmaceutical University, Kyoto 607-8412, JapanDepartment of Neurobiology, Kyoto Pharmaceutical University, Kyoto 607-8412, JapanDepartment of Neurobiology, Kyoto Pharmaceutical University, Kyoto 607-8412, JapanDepartment of Neurobiology, Kyoto Pharmaceutical University, Kyoto 607-8412, JapanDepartment of Psychopharmacology, Central Institute of Mental Health, Mannheim 68159, GermanyDepartment of Neurology, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, JapanIn Alzheimer’s disease, fibrillar amyloid-β (Aβ) peptides form senile plaques associated with microglia. However, the relationship between Aβ peptides and microglia is not fully understood. In this study, the incubation of Aβ1-40 (Aβ40) produced small oligomers, while incubation with Aβ1-42 (Aβ42) caused large molecular aggregates. Microglial production of nitrite, interleukin-6 and tumor necrosis factor-a was induced by Aβ40, but not Aβ42. This production was significantly reduced by 15-deoxy-Δ12,14 prostaglandin J2, and it was completely suppressed by β-sheet breaker peptide, Leu-Pro-Phe-Phe-Asp. These results suggest that small oligomers, rather than large molecular aggregates, mediate microglial activation induced by Aβ peptides.http://www.sciencedirect.com/science/article/pii/S1347861319327161 |
| spellingShingle | Kazuyuki Takata Yoshihisa Kitamura Masaaki Umeki Daiju Tsuchiya Jun-ichi Kakimura Takashi Taniguchi Peter J. Gebicke-Haerter Shun Shimohama Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial Activation Journal of Pharmacological Sciences |
| title | Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial Activation |
| title_full | Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial Activation |
| title_fullStr | Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial Activation |
| title_full_unstemmed | Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial Activation |
| title_short | Possible Involvement of Small Oligomers of Amyloid-β Peptides in 15-Deoxy-Δ 12,14 Prostaglandin J2-Sensitive Microglial Activation |
| title_sort | possible involvement of small oligomers of amyloid β peptides in 15 deoxy δ 12 14 prostaglandin j2 sensitive microglial activation |
| url | http://www.sciencedirect.com/science/article/pii/S1347861319327161 |
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