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Literature summary extracted from

  • Zou, M.H.; Wu, Y.
    AMP-activated protein kinase activation as a strategy for protecting vascular endothelial function (2008), Clin. Exp. Pharmacol. Physiol., 35, 535-545.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.31 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside AICAR, activates AMPK, wherby altering the expression of a variety of genes, including those for uncoupling protein (UCP)-3 and GLUT-4 in muscle, and fatty acid synthase and phosphoenolpyruvate carboxykinase in hepatocytes Rattus norvegicus
2.7.11.31 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside AICAR, increases AMPK activity Homo sapiens
2.7.11.31 additional information AMPK may be sensitive to the lipid status of a cell and activation may be influenced by intracellular fatty acid availability independent of cellular AMP levels Rattus norvegicus
2.7.11.31 additional information LKB1, a serine-threonine kinase of 433 amino acids, which contains both a kinase domain and a nuclear localization signal in its N-terminal region, phosphorylates the T-loop of AMPK Homo sapiens
2.7.11.31 additional information protein kinases Elm1, Pak1 and Tos3 phosphorylate and activate SNF1 Saccharomyces sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.31 additional information protein phosphatase 2A (PP2A) and protein phosphatase 2C (PP2C) inactivate the active and phosphorylated form of AMPK in cell-free assays. Dephosphorylation of AMPK by PP2Calpha is inhibited by 5'-AMP Homo sapiens
2.7.11.31 additional information AMPK phosphorylation is significantly reduced in ob/ob mouse hearts compared with lean, wild-type controls and the reduction in active phosphorylated AMPKalpha is associated with an increase in protein phosphatase 2C (PP2C) Mus musculus
2.7.11.31 additional information AMPK phosphorylation is significantly reduced in Zucker diabetic fa/fa rats compared with lean, wild-type controls and the reduction in active phosphorylated AMPKalpha is associated with an increase in protein phosphatase 2C (PP2C). AMPK activity is reduced in aortic endothelium or skeletal muscle of obese rats compared with lean animals. Possibility that chronic exposure of cells to fatty acids may inhibit AMPK activation. Feeding of a high fat diet significantly decreases AMPK in the liver and muscles Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.31 Mg2+
-
Mus musculus
2.7.11.31 Mn2+
-
Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.31 Homo sapiens
-
-
-
2.7.11.31 Mus musculus
-
-
-
2.7.11.31 Rattus norvegicus
-
-
-
2.7.11.31 Saccharomyces sp.
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.31 3T3-L1 cell
-
Mus musculus
-
2.7.11.31 aorta endothelium
-
Rattus norvegicus
-
2.7.11.31 endothelial cell
-
Homo sapiens
-
2.7.11.31 heart
-
Mus musculus
-
2.7.11.31 hepatocyte
-
Rattus norvegicus
-
2.7.11.31 HUVEC cell
-
Homo sapiens
-
2.7.11.31 liver expresses both alpha1 and alpha2 isoforms Rattus norvegicus
-
2.7.11.31 muscle
-
Homo sapiens
-
2.7.11.31 muscle
-
Rattus norvegicus
-
2.7.11.31 pericyte
-
Homo sapiens
-
2.7.11.31 preadipocyte
-
Mus musculus
-
2.7.11.31 retina
-
Homo sapiens
-
2.7.11.31 smooth muscle
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.31 ATP + 3-hydroxy-3-methyl-glutaryl-CoA reductase
-
Rattus norvegicus ADP + [3-hydroxy-3-methyl-glutaryl-CoA reductase]phosphate
-
?
2.7.11.31 ATP + acetyl-CoA carboxylase
-
Rattus norvegicus ADP + [acetyl-CoA carboxylase]phosphate
-
?
2.7.11.31 ATP + glycerophosphate acyltransferase
-
Rattus norvegicus ADP + [glycerophosphate acyltransferase]phosphate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.31 AMP-activated protein kinase
-
Mus musculus
2.7.11.31 AMP-activated protein kinase
-
Homo sapiens
2.7.11.31 AMP-activated protein kinase
-
Rattus norvegicus
2.7.11.31 AMPK
-
Mus musculus
2.7.11.31 AMPK
-
Homo sapiens
2.7.11.31 AMPK
-
Rattus norvegicus
2.7.11.31 Snf1 yeast homolog of mammalian AMPK Saccharomyces sp.

General Information

EC Number General Information Comment Organism
2.7.11.31 physiological function AMPK activation alters the expression of a variety of genes, including phosphoenolpyruvate carboxykinase in hepatocytes. Reduced AMPK activation may play an important role in the lipid accumulation and genesis of endothelial dysfunction in obese rats. Endothelial AMPK activity may inhibit glycerol-3-phosphate acyltransferase, required for de novo synthesis of diacylglycerol Rattus norvegicus
2.7.11.31 physiological function AMPK may play an important role in protecting endothelial cells against adverse effects of sustained hyperglycaemia, such as alterations in fatty acid metabolism, impaired Akt activation by insulin, increased caspase 3 activity and apoptosis. It may modulate endothelial cell energy supply. The AMPK-acetyl CoA carboxylase-malonyl CoA-carnitine palmitoyl-transferase 1 mechanism for regulating long-chain fatty acid oxidation, similar to that of muscle, operates in the endothelial cell and is regulated by AMPK under physiological conditions. One way to deal with endothelial lipotoxicity is to promote free fatty acid oxidation and ameliorate lipid accumulation in endothelial cells, which can be achieved by activating endothelial AMPK. AMPK inhibits fatty acid-induced increases in NF-kappaB transactivation in cultured human umbilical vein endothelial cells Homo sapiens