Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200611
Type: Artigo de periódico
Title: Hypothalamic Inhibition Of Acetyl-coa Carboxylase Stimulates Hepatic Counter-regulatory Response Independent Of Ampk Activation In Rats.
Author: Santos, Gustavo A
Pereira, Vinícius D
Roman, Erika A F R
Ignacio-Souza, Leticia
Vitorino, Daniele C
de Moura, Rodrigo Ferreira
Razolli, Daniela S
Torsoni, Adriana S
Velloso, Licio A
Torsoni, Marcio A
Abstract: Hypothalamic AMPK acts as a cell energy sensor and can modulate food intake, glucose homeostasis, and fatty acid biosynthesis. Intrahypothalamic fatty acid injection is known to suppress liver glucose production, mainly by activation of hypothalamic ATP-sensitive potassium (K(ATP)) channels. Since all models employed seem to involve malonyl-CoA biosynthesis, we hypothesized that acetyl-CoA carboxylase can modulate the counter-regulatory response independent of nutrient availability. In this study employing immunoblot, real-time PCR, ELISA, and biochemical measurements, we showed that reduction of the hypothalamic expression of acetyl-CoA carboxylase by antisense oligonucleotide after intraventricular injection increased food intake and NPY mRNA, and diminished the expression of CART, CRH, and TRH mRNA. Additionally, as in fasted rats, in antisense oligonucleotide-treated rats, serum glucagon and ketone bodies increased, while the levels of serum insulin and hepatic glycogen diminished. The reduction of hypothalamic acetyl-CoA carboxylase also increased PEPCK expression, AMPK phosphorylation, and glucose production in the liver. Interestingly, these effects were observed without modification of hypothalamic AMPK phosphorylation. Hypothalamic ACC inhibition can activate hepatic counter-regulatory response independent of hypothalamic AMPK activation.
Subject: Amp-activated Protein Kinases
Acetyl-coa Carboxylase
Animals
Body Weight
Diet
Gene Expression Regulation
Gluconeogenesis
Hormones
Hypothalamus
Liver
Male
Oligonucleotides
Phosphorylation
Rats
Rights: aberto
Identifier DOI: 10.1371/journal.pone.0062669
Address: http://www.ncbi.nlm.nih.gov/pubmed/23626844
Date Issue: 2013
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

Files in This Item:
File SizeFormat 
pmed_23626844.pdf773.3 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.