Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction
| Autor: | Masha G. Savelieff, Juhye Kang, Elizabeth M. Nolan, Hyuck Jin Lee, Shin Jung C. Lee, Toshiki G. Nakashige, Megan Brunjes Brophy, Mi Hee Lim |
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| Přispěvatelé: | Massachusetts Institute of Technology. Department of Chemistry |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Metal ions in aqueous solution Biophysics S100 Calcium Binding Protein beta Subunit Protein aggregation 010402 general chemistry 01 natural sciences Biochemistry Oligomer S100A9 S100A8 Biomaterials Metal 03 medical and health sciences chemistry.chemical_compound Neuroblastoma Protein Aggregates Tumor Cells Cultured Humans Amyloid beta-Peptides Metals and Alloys In vitro 0104 chemical sciences 030104 developmental biology chemistry Chemistry (miscellaneous) Metals visual_art visual_art.visual_art_medium Calprotectin Leukocyte L1 Antigen Complex |
| Zdroj: | Prof. Nolan via Ye Li |
| ISSN: | 1756-591X |
| Popis: | Proteins from the S100 family perform numerous functions and may contribute to Alzheimer's disease (AD). Herein, we report the effects of S100A8/S100A9 heterooligomer calprotectin (CP) and the S100B homodimer on metal-free and metal-bound amyloid-β (Aβ; Aβ 40 and Aβ 42 ) aggregation in vitro. Studies performed with CP-Ser [S100A8(C42S)/S100A9(C3S) oligomer] indicate that the protein influences the aggregation profile for Aβ 40 in both the absence and presence of metal ions [i.e., Zn(ii) and Cu(ii)]. Moreover, the detection of Aβ 40 -CP-Ser complexes by mass spectrometry suggests a direct interaction as a possible mechanism for the involvement of CP in Aβ 40 aggregation. Although the interaction of CP-Ser with Aβ 40 impacts Aβ 40 aggregation in vitro, the protein does not attenuate Aβ-induced toxicity in SH-SY5Y cells. In contrast, S100B has a slight effect on the aggregation of Aβ. Overall, this work supports a potential association of CP with Aβ in the absence and presence of metal ions in AD. |
| Databáze: | OpenAIRE |
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