Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Twelve enzymes related to the direct oxidative and glycolytic pathways of glucose metabolism were assayed in 88 cancers of the cervix and 48 cancers of the endometrium of the human uterus, and the activities compared with those obtained from a group of control tissues. Significant increases for all but one of the enzymes studied (alpha-glycerolphosphate dehydrogenase) were found in cancer of the cervix, when compared with normal cervix epithelium. Hexokinase, phoshofructokinase, and aldolase appear to be rate-limiting in normal cervix epithelium; however, since the increase in activity of the first two in cancers was least of all the glycolytic enzymes, redundant enzyme synthesis probably occurs in the malignant cell for the enzymes catalysing reversible reactions. There was virtually no correlation between the activity of any enzyme measured in the cancer sample and histological assessments of the degree of malignancy of the tumour, or the clinical stage of the disease. All enzymes except pyruvate kinase had significantly higher activity in normal endometrium than in normal cervix epithelium, presumably reflecting the greater metabolic requirements of the former tissue. Only phosphoglucose isomerase and pyruvate kinase were significantly higher in endometrial cancer than in normal endometrium, and there were few significant differences between cancers of the cervix and of the endometrium, despite the marked differences in their tissues of origin. These results suggest the changes occur during malignant transformation to the activities of both regulatory enzymes and those catalysing reversible reactions, in a manner justifying the conclusion that the general metabolism of tumours is convergent.
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PMID:Enzymes of glucose metabolism in carcinoma of the cervix and endometrium of the human uterus. 67 39

ATPase activity of uterus and ovary was markedly elevated in presence of gossypol and decreased in presence of lactic acid indicating activation and inhibition of energy metabolism by gossypol and lactic acid respectively. The elevated levels of glycogen in uterus indicate inhibition of glycogenolysis as supported by phosphorylase activity. Whereas in ovary the glycogen depletion indicates activation of glycogenolysis supported by phosphorylase activity. The activity levels of aldolase and G-6-PDH decreased in the uterus in presence of gossypol and increased in presence of lactic acid. The same were elevated in ovary indicating the activation of hexose mono and diphosphate pathways. Lactic acid accumulated in presence of both gossypol and lactic acid with a depletion in level of pyruvic acid in both the tissues. This situation in the uterus indicates the condition of anti-implantation in presence of both gossypol and lactic acid. The NAD-LDH activity was inhibited in presence of gossypol and activated in presence of lactic acid in both tissues.
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PMID:In vitro effects of gossypol and lactic acid on rat uterus and ovary during implantation and antiimplantation. 263 59

The inactivating action of a lysosome-enriched fraction on oestradiol receptors from rat uterus cytosol under in vitro conditions is reported. During incubation at 25 degrees C in the absence of oestradiol, the inactivation of the oestradiol receptor depends directly on the amount of lysosome-enriched fraction present. Boiled lysosome-enriched fractions have no effect on cytosol receptors. The inactivation of oestradiol receptors was maximal when the incubation was performed at pH 7.5 and follows second order kinetics. Progesterone receptors were also lost during the incubation but two other proteins present in cytosol (aldolase and lactate dehydrogenase) show almost no change in amount during the procedure. It appears that the inactivating process reflects the action of quite specific entities present in the lysosome-enriched fraction. The effect of the lysosome-enriched fraction on cytosol oestradiol receptors is quantitative as judged from unchanged KA value and electrophoretic mobility of the surviving receptors.
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PMID:In vitro inactivation of the oestradiol receptor by a lysosome-enriched fraction from rat uterus. 729 60