Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1) In intact Ehrlich ascites tumour cells the anaerobic glycolytic flux rate and pattern of intermediates have been investigated at different pH values of the extracellular medium. 2) As predicted from the dependence of the lactic acid dehydrogenase equilibrium on pH a strong negative correlation between log ([lactate]/[pyruvate]) and pH has been found. 3) The steady state fluxes of glycolysis at pH 8.0 and 7.4 are rather equal, despite significant differences in the intracellular concentrations of glycolytic intermediates. At pH 8.0 the concentrations of ATP, glucose 6-phosphate, and fructose 6-phosphate are lower, and the concentrations of ADP, AMP, fructose 1,6-bisphosphate, triose phosphates, phosphoglycerates, and phosphoenolpyruvate are higher than at pH 7.4. 4) From the analysis of the pH dependent changes of metabolites it follows that different mechanisms are responsible for maintaining equal actual activities of hexokinase, phosphofructokinase and pyruvate kinase at pH 7.4 and 8.0. 5) From an application of the linear theory of enzymatic chains and a calculation of the control strength of the regulatory important enzymes results that hexokinase is evidently rate-limiting for glycolysis, and phosphofructokinase is also significantly influencing the glycolytic flux. Pyruvate kinase and glyceraldehyde phosphate dehydrogenase, on the other hand, do not significantly affect the rate of the overall glycolytic flux in ascites.
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PMID:Regulation of anaerobic glycolysis in Ehrlich ascites tumour cells. 2 29

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.
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PMID:Regulation of glycolysis and oxygen consumption in lymph-node cells of normal and leukaemic mice. 645 31

To investigate the role of C16:0 ceramide in melanoma metastatic behavior and glycolysis, five common long-chain ceramides (C16:0, C18:0, C20:0, C22:0, C24:0) were tested in melanocyte and melanoma cell lines by LC-MS. We then treated non-metastatic and metastatic melanoma cells with PDMP and exogenous C16:0 to explore their effects on proliferation, migration, and glycolysis. The long-chain ceramide was also analyzed by LC-MS after treatment. C16:0 ceramide showed the highest levels in melanocyte and melanoma cells, with all melanomas higher than melanocytes. PDMP inhibited malignant behavior and glycolysis in melanoma, and caused the accumulation of intracellular C16:0. Exogenous C16:0 promoted melanoma glycolysis, but not malignant behavior, and decreased intracellular C16:0. Finally, pyruvate kinase (PK), hexokinase (HK), and lactic acid dehydrogenase (LDH) activity, key enzymes in glycolysis, were altered after treatment with PDMP and exogenous C16:0.
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PMID:C16:0 ceramide effect on melanoma malignant behavior and glycolysis depends on its intracellular or exogenous location. 3226 39