Literature summary for 2.7.11.27 extracted from

Santos, G.A.; Pereira, V.D.; Roman, E.A.; Ignacio-Souza, L.; Vitorino, D.C.; de Moura, R.F.; Razolli, D.S.; Torsoni, A.S.; Velloso, L.A.; Torsoni, M.A.
Hypothalamic inhibition of acetyl-CoA carboxylase stimulates hepatic counter-regulatory response independent of AMPK activation in rats (2013), PLoS ONE, 8, e62669.

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Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-
Rattus norvegicus Wistar	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	determination of levels of hypothalamic phosphorylation of AMPK	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining
hypothalamus	determination of levels of hypothalamic phosphorylation of AMPK	Rattus norvegicus	-

Synonyms

Synonyms	Comment	Organism
AMPK	-	Rattus norvegicus

General Information

General Information	Comment	Organism
metabolism	the reduction of hypothalamic acetyl-CoA carboxylase increases phophoenolpyruvate carboxykinase expression, AMPK phosphorylation, and glucose production in the liver. These effects are observed without modification of hypothalamic AMPK phosphorylation. Fasted rats show greater AMPK phosphorylation levels than fed rats. Reduced AMPK phosphorylation is linked to an increase in acetyl-CoA carboxylase activity and biosynthesis of malonyl-CoA	Rattus norvegicus
physiological function	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	Rattus norvegicus

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Release 2023.1 (January 2023)