| Registro completo |
| Provedor de dados: |
Anais da ABC (AABC)
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| País: |
Brazil
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| Título: |
Amyloid-β peptide absence in short term effects on kinase activity of energy metabolism in mice hippocampus and cerebral cortex
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| Autores: |
IANISKI,FRANCINE R.
RECH,VIRGINIA C.
NISHIHIRA,VIVIAN S.K.
ALVES,CATIANE B.
BALDISSERA,MATHEUS D.
WILHELM,ETHEL A.
LUCHESE,CRISTIANE
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| Data: |
2016-01-01
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| Ano: |
2016
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| Palavras-chave: |
Alzheimer's disease
Nanoparticles
Meloxicam
Energetic metabolism
Phosphoryltransfer network
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| Resumo: |
ABSTRACT 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-β 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-β 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-β, 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-β. In conclusion we observed absence in short-term effects in kinases activities of energy metabolism in mice hippocampus and cerebral cortex using amyloid-β 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.
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| Tipo: |
Info:eu-repo/semantics/article
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000501829
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| Editor: |
Academia Brasileira de Ciências
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| Relação: |
10.1590/0001-3765201620150776
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| Formato: |
text/html
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| Fonte: |
Anais da Academia Brasileira de Ciências v.88 n.3 suppl.0 2016
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| Direitos: |
info:eu-repo/semantics/openAccess
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