Plasmalogens Alter the Aggregation Rate of Transthyretin and Lower Toxicity of Transthyretin Fibrils.
J Phys Chem Lett
; 15(17): 4761-4766, 2024 May 02.
Article
en En
| MEDLINE
| ID: mdl-38661515
ABSTRACT
Heart tissue can experience a progressive accumulation of transthyretin (TTR), a small four subunit protein that transports holoretinol binding protein and thyroxine. This severe pathology is known as transthyretin amyloid cardiomyopathy. Numerous experimental studies indicated that the aggregation rate and toxicity of TTR fibrils could be altered by the presence of lipids; however, the role of plasmalogens in this process remains unknown. In this study, we investigate the effect of choline plasmalogens (CPs) with different lengths and saturations of fatty acids (FAs) on TTR aggregation. We found that CPs with saturated and unsaturated FAs strongly suppressed TTR aggregation. We also found that CPs with saturated FAs did not change the morphology of TTR fibrils; however, much thicker fibrillar species were formed in the presence of CPs with unsaturated FAs. Finally, we found that CPs with C160, C180, and C181 FAs substantially lowered the cytotoxicity of TTR fibrils that were formed in their presence.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Prealbúmina
/
Plasmalógenos
Límite:
Humans
Idioma:
En
Revista:
J Phys Chem Lett
Año:
2024
Tipo del documento:
Article
País de afiliación:
Estados Unidos