title: Shedding Light on Fat Dependence in AML.
abstract: Scientists have begun unraveling the molecular intricacies that drive the appetite of acute myeloid leukemia for fat. They found that these tumor cells have particularly low levels of PHD3, an enzyme that normally activates ACC2 to repress fatty-acid oxidation. This fuels the cells' metabolic reliance on fat-burning, but also renders them highly susceptible to inhibitors of fatty-acid oxidation.
mesh_terms: D000103:Acetyl-CoA Carboxylase / Q000378:metabolism; D000263:Adenylate Kinase / Q000378:metabolism; D004852:Epoxy Compounds / Q000494:pharmacology; D006801:Humans; D064799:Hypoxia-Inducible Factor-Proline Dioxygenases / Q000378:metabolism; D015470:Leukemia, Myeloid, Acute / Q000378:metabolism*; D050356:Lipid Metabolism / Q000187:drug effects; D010084:Oxidation-Reduction / Q000187:drug effects; D010766:Phosphorylation; D000069458:Ranolazine / Q000494:pharmacology; D014407:Tumor Cells, Cultured
chemical_list: D004852:Epoxy Compounds; D000069458:Ranolazine; C488894:EGLN3 protein, human; D064799:Hypoxia-Inducible Factor-Proline Dioxygenases; D000263:Adenylate Kinase; C520105:ACACB protein, human; D000103:Acetyl-CoA Carboxylase; C054207:etomoxir