Amyloid-ß peptide absence in short term effects on kinase activity of energy metabolism in mice hippocampus and cerebral cortex.
An Acad Bras Cienc
; 88(3 Suppl): 1829-1840, 2016.
Article
em En
| MEDLINE
| ID: mdl-27411072
Considering that Alzheimer's disease is a prevalent neurodegenerative disease worldwide, we investigated the activities of three key kinases: creatine kinase, pyruvate kinase and adenylate kinase in the hippocampus and cerebral cortex in Alzheimer's disease model. Male adult Swiss mice received amyloid-ß or saline. One day after, mice were treated with blank nanocapsules (17 ml/kg) or meloxicam-loaded nanocapsules (5 mg/kg) or free meloxicam (5 mg/kg). Treatments were performed on alternating days, until the end of the experimental protocol. In the fourteenth day, kinases activities were performed. Amyloid-ß did not change the kinases activity in the hippocampus and cerebral cortex of mice. However, free meloxicam decrease the creatine kinase activity in mitochondrial-rich fraction in the group induced by amyloid-ß, but for the cytosolic fraction, it has raised in the activity of pyruvate kinase activity in cerebral cortex. Further, meloxicam-loaded nanocapsules administration reduced adenylate kinase activity in the hippocampus of mice injected by amyloid-ß. In conclusion we observed absence in short-term effects in kinases activities of energy metabolism in mice hippocampus and cerebral cortex using amyloid-ß peptide model. These findings established the foundation to further study the kinases in phosphoryltransfer network changes observed in the brains of patients post-mortem with Alzheimer's disease.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Piruvato Quinase
/
Córtex Cerebral
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Adenilato Quinase
/
Peptídeos beta-Amiloides
/
Creatina Quinase
/
Metabolismo Energético
/
Doença de Alzheimer
/
Hipocampo
Tipo de estudo:
Guideline
/
Prognostic_studies
Limite:
Animals
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Humans
/
Male
Idioma:
En
Revista:
An Acad Bras Cienc
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Brasil