1'-Acetoxychavicol Acetate Increases Proteasome Activity by Activating cAMP-PKA Signaling.
Planta Med
; 84(3): 153-159, 2018 Feb.
Article
em En
| MEDLINE
| ID: mdl-28859215
ABSTRACT
Protein degradation systems are critical pathways for the maintenance of protein homeostasis. The age-dependent attenuation of the proteasome activity contributes to age-related neurodegenerative processes. The molecule 1'-acetoxychavicol acetate (ACA) is naturally obtained from the rhizomes and seeds of Zingiberaceae plants, such as Languas galangal and Alpinia galangal, and exhibits anti-carcinogenic effects. Recently, we have shown that ACA protected the age-related learning and memory impairments in senescence-accelerated mice and maintained cognitive performance. Therefore, we here examined the effects of ACA on the protein degradation systems and cell protection against neurotoxicity in differentiated PC12 cells. ACA increased proteasome activity in PC12 cells. Increased proteasome activity occurred during the initial stages of ACA treatment and lasted at least 9 h. The activity returned to control levels within 24 h. The increase in proteasome activity by ACA was suppressed by H-89, which is a cAMP-dependent protein kinase A inhibitor. ACA increased the adenylate cyclase activity and therefore the intracellular cAMP levels. Furthermore, ACA recovered the initial cell viability, which was reduced after the addition of the amyloid ß-protein fragment to neuronally differentiated PC12 cells. The effects of ACA on amyloid toxicity were reduced after treatment with MG132, a proteasome inhibitor. These results demonstrated a neuroprotective effect of ACA via activation of cAMP/cAMP-dependent protein kinase A signaling in neuronally differentiated PC12 cells.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Álcoois Benzílicos
/
Proteínas Quinases Dependentes de AMP Cíclico
/
Complexo de Endopeptidases do Proteassoma
Limite:
Animals
Idioma:
En
Revista:
Planta Med
Ano de publicação:
2018
Tipo de documento:
Article