hexokinase/sarcoma

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[A study of hexokinase isoenzymes in rat sarcoma M-1].

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Using a wide spectrum of criteria, the isozyme composition of hexokinase from sarcoma M-1 reinoculated to rat m. gastrocnemius was studied. The structural, physicochemical and functional properties of the homogeneous enzyme which is represented in sarcoma M-1 by one molecular form, were

[Adsorption mechanism of hexokinase activity regulation in rat sarcoma M-1].

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The hexokinase interaction with mitochondrial membranes in rat sarcoma M-1 cells was studied. The conditions of formation of the enzyme complex with mitochondrial membranes and its stability were elaborated. The kinetic parameters of free and membrane-bound hexokinases were determined. The data

[Subcellular localization, isoenzyme spectrum and properties of hexokinase from sarcoma M-1].

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In sarcoma M-I the hexokinase activity was found to exceed three-fold the enzyme activity in muscular tissue. In the muscles and tumor intracellular distribution of hexokinase was essentially the same; the main part of the enzyme was localized in hyaloplasma. The mitochondrial hexokinase from

Classical NF-κB Metabolically Reprograms Sarcoma Cells Through Regulation of Hexokinase 2.

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UNASSIGNED Metabolic reprogramming has emerged as a cancer hallmark, and one of the well-known cancer-associated metabolic alterations is the increase in the rate of glycolysis. Recent reports have shown that both the classical and alternative signaling pathways of nuclear factor κB (NF-κB) play

Enzyme changes induced in normal and malignant tissues with chemical agents. IV. Effect of alpha-peltatin on glucose utilization by sarcoma 37 and on the adenosinetriphosphatase, hexokinase, aldolase, and pyridine nucleotide levels of sarcoma 37.

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The action of nitrogen mustards on the glycolysis and hexokinase activity of rat reticulo-sarcoma ascites cells.

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[Hexokinase, aspartate and alanine aminotransferase activity in transplanted rat sarcomas].

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Hexose transport in sarcoma virus transformed cells.

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Avian and mammalian fibroblast cultures transformed by type C sarcoma viruses show a dramatic enhancement of the rate of hexose transport at the beginning of transformation which is quantitatively and qualitatively different from that seen by variation in culture conditions of nontransformed control

Transport and phosphorylation of hexoses in normal and Rous sarcoma virus-transformed chick embryo fibroblasts.

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Effects of transformation by Rous sarcoma virus on sugar uptake and activity and the subcellular distribution of hexokinase isozymes in chick embryo fibroblasts were examined. Transformation caused a several-fold increase in the maximum velocity for uptake of 2-deoxyglucose without a significant

Enzymes and nucleotides in virions of Rous sarcoma virus.

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In addition to the previously described deoxyribonucleic acid (DNA) polymerase, DNA ligase, DNA exonuclease, and DNA endonuclease activities, purified virions of Schmidt-Ruppin strain of Rous sarcoma virus (SRV) have nucleotides and nucleotide kinase, phosphatase, hexokinase, and lactate

[The characteristics of sarcoma M-1 in rats].

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Some biochemical characteristics of rat sarcoma M-1 transplanted into skeletal muscle have been investigated. Data on the key enzyme activity of the carbohydrate metabolism on the different stages of neoplasia are reported. The isozyme content and intracellular location of hexokinase in sarcoma M-1

[Brain metabolism of sarcoma 45-bearing rats undergoing radiation and the effect of hyperthermia on the tumor].

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Activity of hexokinase and acetylcholinesterase and pyridoxal co-enzyme content of brain subcellular fractions were studied in rats, bearing sarcoma 45, after local exposure of the tumor to 20 Gy X-radiation and microwave hyperthermia. The carbohydrate metabolism was sharply inhibited while the

Inhibition of hexokinase and protein kinase activities of tumor cells by a chloromethyl ketone derivative of lactic acid.

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A chloromethyl ketone derivative of lactic acid is a potent inhibitor of glycolysis of Ehrlich ascites tumor cells. It inhibited glycolysis of intact cells by about 50% at 200 microM (100 nmol/mg of protein) while cell-free extracts were inhibited 50% at 50 microM (50 nmol/mg of protein). N

Alterations in glucose metabolism in chick-embryo cells transformed by Rous sarcoma virus: intracellular levels of glycolytic intermediates.

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Chick-embryo cells, transformed with Rous sarcoma virus, show enhanced rates of sugar transport and glycolysis. Determination of intracellular concentrations of glycolytic intermediates suggests that the enhanced glycolytic flux is due to increased activities of hexokinase (ATP:D-hexose

Activity of hexokinase is increased by its interaction with hepatitis C virus protein NS5A.

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The study of cellular central carbon metabolism modulations induced by viruses is an emerging field. Human cytomegalovirus (HCMV), herpes simplex virus (HSV), Kaposi's sarcoma-associated herpesvirus (KSHV), and hepatitis C virus (HCV) have been shown recently to reprogram cell metabolism to support

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