β Amyloid peptide (Aβ42) is internalized via the G‐protein‐coupled receptor FPRL1 and forms fibrillar aggregates in macrophages1
| Autor: | Chou Chi H. Li, Takeda, Victor J. Ferrans, Ji Ming Wang, Joost J. Oppenheim, Zu-Xi Yu, Wanghua Gong, Hiroshi Yazawa, Yingying Le |
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| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Microglia Amyloid Chemistry media_common.quotation_subject P3 peptide Peptide Biochemistry Cell biology Proinflammatory cytokine medicine.anatomical_structure Genetics medicine Receptor Internalization Molecular Biology Biotechnology G protein-coupled receptor media_common |
| Zdroj: | The FASEB Journal. 15:2454-2462 |
| ISSN: | 1530-6860 0892-6638 |
| Popis: | The 42 amino acid form of β amyloid (Aβ42) plays a pivotal role in neurotoxicity and the activation of mononuclear phagocytes in Alzheimer’s disease (AD). Our recent study revealed that FPRL1, a G-protein-coupled receptor, mediates the chemotactic and activating effect of Aβ42 on mononuclear phagocytes (monocytes and microglia), suggesting that FPRL1 may be involved in the proinflammatory responses in AD. We investigated the role of FPRL1 in cellular uptake and the subsequent fibrillar formation of Aβ42 by using fluorescence confocal microscopy. We found that upon incubation with macrophages or HEK293 cells genetically engineered to express FPRL1, Aβ42 associated with FPRL1 and the Aβ42/FPRL1 complexes were rapidly internalized into the cytoplasmic compartment. The maximal internalization of Aβ42/FPRL1 complexes occurred by 30 min after incubation. Removal of free Aβ42 from culture supernatants at 30 min resulted in a progressive recycling of FPRL1 to the cell surface and degradation of the internalized A... |
| Databáze: | OpenAIRE |
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