Data/hora: 13/06/2024 00:41:05

Provedor de dados: 	42	
País: 	Brazil	
Título: 	Amyloid-β peptide absence in short term effects on kinase activity of energy metabolism in mice hippocampus and cerebral cortex	
Autores: 	IANISKI,FRANCINE R.; RECH,VIRGINIA C.; NISHIHIRA,VIVIAN S.K.; ALVES,CATIANE B.; BALDISSERA,MATHEUS D.; WILHELM,ETHEL A.; LUCHESE,CRISTIANE.	
Data: 	2016-01-01	
Ano: 	2016	
Palavras-chave: 	Alzheimer's disease; Nanoparticles; Meloxicam; Energetic metabolism; Phosphoryltransfer network.	
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.	
Tipo: 	Info:eu-repo/semantics/article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652016000501829	
Editor: 	Academia Brasileira de Ciências	
Relação: 	10.1590/0001-3765201620150776	
Formato: 	text/html	
Fonte: 	Anais da Academia Brasileira de Ciências  v.88 n.3 suppl.0 2016	
Fonte: 	info:eu-repo/semantics/openAccess