Regulation of glycolysis and oxygen consumption in lymph-node cells of normal and leukaemic mice.
Lymph-node cells of (AKR X C3H) F1 leukaemic mice showed a considerable increase of glycolytic activity and O2 consumption. The glycolytic enzymes phosphofructokinase, pyruvate kinase, aldolase and lactic acid dehydrogenase showed increased activities in leukaemic conditions. Studies on permeabilized leukaemic and normal lymph-node cells, and assays on partially purified phosphofructokinase and pyruvate kinase enzymes, revealed that the enhanced glycolysis of the tumour cells was due to the predominance of glycolytic isoenzymes relatively insensitive to the natural metabolic inhibitors. The glycolytic enzyme hexokinase showed decreased activity in leukaemic conditions, owing to a subcellular translocation of its bulk from the cytosol to the mitochondrial fraction. Association of hexokinase with the mitochondria accounted for an ATPase-like stimulatory action on cell respiration which can explain the increased O2 uptake of leukaemic cells.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005260:Female; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D006019:Glycolysis; D006593:Hexokinase / Q000378:metabolism; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D007942:Leukemia, Experimental / Q000378:metabolism*; D008198:Lymph Nodes / Q000378:metabolism*; D051379:Mice; D010101:Oxygen Consumption; D010732:Phosphofructokinase-1 / Q000378:metabolism; D011770:Pyruvate Kinase / Q000378:metabolism
D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase; D006593:Hexokinase; D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase; D005634:Fructose-Bisphosphate Aldolase