Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0345904 (liver cancer)
 15,188 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A method for the assay of glycylproline dipeptidyl aminopeptidase activity in the serum is described. The enzyme activity determination in sera from patients with hepatic cancer opens a possibility in the differential diagnosis of hepatobiliary diseases, because of the significantly higher values found in some cases of hepatic cancer. No correlation with alpha-fetoprotein was found.
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PMID:Serum glycylproline dipeptidyl aminopeptidase activity in human hepatic cancer. 44 39

Multiforms of aminopeptidases and arylamidases in normal human liver, stomach, lung, ileum, colon, rectum, and kidney, and cancer tissue from human liver, stomach, and lung were separated by triethylaminoethyl cellulose column chromatography. The aminopeptidases and arylamidases were solubilized from human tissues by treatment with bromelain, and their column chromatograms on triethylaminoethyl-cellulose gave different patterns of multiforms of enzymes in these tissues. The fractions of enzymes separated specificities toward L-leucyl-beta-naphthylamide, L-leucinamide, L-methioninamide, L-phenylalaninamide, and L-alaninamide. The activity of aminopeptidase toward L-leucinamide and of arylamidase toward L-leucyl-beta-naphthylamide was higher in human stomach cancer tissue and lower in hepatic cancer tissue than in normal stomach and liver, respectively. In lung cancer tissue, the activity of aminopeptidase toward L-leucinamide was abnormally low, while the activity of arylamidase toward L-leucyl-beta-napthylamide was similar to that in normal lung. The substrate specificities or patterns of the multiforms of these enzymes in cancer tissue from human liver, stomach, and lung were shown to differ from those of normal liver, stomach, and lung, respectively, by triethylaminoethyl cellulose column chromatography.
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PMID:Aminopeptidases and arylamidases in normal and cancer tissues in humans. 111 41

Changes of glycylproline dipeptidyl aminopeptidase (GPDA) and gamma-glutamyl transpeptidase (gamma-GTP) activities and their subcellular distributions were compared in human hepatic cancer and embryonal tissues. The activity of GPDA in cancer tissues was significantly higher than that found in healthy liver, though there were no significant differences between fetal and adult livers. The placenta, however, had the highest GPDA activity. The activity of gamma-GTP, on the other hand, was increased significantly not only in cancer tissues but also in live tissues adjacent to the tumor, and it was higher in the fetal liver but much lower in the placenta. Subcellular distribution of GPDA was also different from that of gamma-GTP in cancer tissues, especially after postmortem changes. These results suggest the possibility that GPDA has carcinoembryonic characters similar to gamma-GTP, but the mechanisms, whereby serum activities of these two enzymes were increased in hepatocellular carcinoma patients, are different from each other.
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PMID:Glycylproline dipeptidyl aminopeptidase and gamma-glutamyl transpeptidase in human hepatic cancer and embryonal tissues. 288 5

Changes of glycylproline dipeptidyl aminopeptidase (GPDA) and gamma-glutamyl transpeptidase (gamma-GTP) activities were compared in the serum and liver tissue of rats with hepatic cancer induced by 3'-methyl DAB. Serum glycylproline dipeptidyl aminopeptidase activity in rats with the azo dye-induced hepatic cancer was significantly higher than that in healthy rats, but the increase was not so extensive compared with that of gamma-glutamyl transpeptidase. The specific activity of glycylproline dipeptidyl aminopeptidase was decrease in the microsomal fraction and increased in the supernatant fraction of hepatic cancer tissue, whereas that of gamma-glutamyl transpeptidase was increased in both microsomal and supernatant fractions. These results suggest that the mechanisms, whereby serum activities of these two enzymes were increased in rats with hepatic cancer, were different from each other.
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PMID:Serum and liver glycylproline dipeptidyl aminopeptidase activity in rats with experimental hepatic cancer. 610 82

Cancer is one of the leading causes of deaths worldwide. While cancers may initially show good response to chemotherapy or radiotherapy, it is not uncommon for them to recur at a later date. This phenomenon may be explained by the existence of a small population of cancer stem cells, which are inherently resistant to anti-cancer treatment as well as being capable of self-renewal. Therefore, while most of the tumour bulk consisting of cells that are not cancer stem cells respond to treatment, the cancer stem cells remain, leading to disease recurrence. Following this logic, the effective targeting of cancer stem cells holds promise for providing long-term cure in individuals with cancer. Cancer stem cells, like normal stem cells are endowed with mechanisms to protect themselves against a wide range of insults including anti-cancer treatments, such as the enhancement of the DNA damage response and the ability to extrude drugs. It is therefore important to develop new strategies if cancer stem cells are to be eradicated. In this review, we describe the strategies that we have developed to target cancer stem cells. These strategies include the targeting of the histone demethylase jumonji, AT rich interactive domain 1B (JARID1B), which we found to be functionally significant in the maintenance of cancer stem cells. Other strategies being pursued include reprogramming of cancer stem cells and the targeting of a functional cell surface marker of liver cancer stem cells, the aminopeptidase CD13.
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PMID:Getting to the heart of the matter in cancer: Novel approaches to targeting cancer stem cells. 2830 61