Calprotectin influences the aggregation of metal-free and metal-bound amyloid-ß by direct interaction.
Metallomics
; 10(8): 1116-1127, 2018 08 15.
Article
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| MEDLINE
| ID: mdl-30046785
ABSTRACT
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-ß (Aß; Aß40 and Aß42) aggregation in vitro. Studies performed with CP-Ser [S100A8(C42S)/S100A9(C3S) oligomer] indicate that the protein influences the aggregation profile for Aß40 in both the absence and presence of metal ions [i.e., Zn(ii) and Cu(ii)]. Moreover, the detection of Aß40-CP-Ser complexes by mass spectrometry suggests a direct interaction as a possible mechanism for the involvement of CP in Aß40 aggregation. Although the interaction of CP-Ser with Aß40 impacts Aß40 aggregation in vitro, the protein does not attenuate Aß-induced toxicity in SH-SY5Y cells. In contrast, S100B has a slight effect on the aggregation of Aß. Overall, this work supports a potential association of CP with Aß in the absence and presence of metal ions in AD.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Péptidos beta-Amiloides
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Complejo de Antígeno L1 de Leucocito
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Subunidad beta de la Proteína de Unión al Calcio S100
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Agregado de Proteínas
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Metales
Límite:
Humans
Idioma:
En
Revista:
Metallomics
Asunto de la revista:
BIOQUIMICA
Año:
2018
Tipo del documento:
Article