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[Significance of pyrimidine nucleoside phosphorylase (PyNPase) and dihydropyrimidine dehydrogenase (DPD) in advanced gastric cancers].

Abstract
We measured pyrimidine nucleoside phosphorylase (PyNPase), a known angiogenetic factor, and dihydropyrimidine dehydrogenase (DPD) in advanced gastric cancers. PyNPase was expressed in cytoplasm of the cancer cells and surrounding interstitial cells. The levels of PyNPase and DPD were significantly higher in cancer tissue. With respect to tumor factors, the level of PyNPase was significantly higher in cases positive for venous invasion. We divided patients into two groups, with high and low activities of IAP and MMP-9. The level of PyNPase was significantly higher in the high IAP activity group. A correlation was suggested between the level of PyNPase and the activity of IAP. 5'-Deoxy-5-fluorouridine (5'-DFUR) is transformed into 5-FU by PyNPase and manifests antitumor effects. DPD is a rate-limiting enzyme in the process of degradation of 5-FU. In the present study, the level of PyNPase/DPD was significantly higher in cancer tissue. PyNPase/DPD suggests not only the malignant potential of the tumor but also the efficiency of chemotherapy using 5-FU, especially 5'-DFUR.
AuthorsS Tsukayama, M Hirano, N Murakami, Y Uno, H Nozawa, H Yoshino, N Orta, H Kikkawa, S Masuda
JournalGan to kagaku ryoho. Cancer & chemotherapy (Gan To Kagaku Ryoho) Vol. 28 Issue 5 Pg. 649-54 (May 2001) ISSN: 0385-0684 [Print] Japan
PMID11383213 (Publication Type: English Abstract, Journal Article)
Chemical References
  • Neoplasm Proteins
  • immunosuppressive acidic protein
  • Oxidoreductases
  • Dihydrouracil Dehydrogenase (NADP)
  • Pentosyltransferases
  • Pyrimidine Phosphorylases
  • Matrix Metalloproteinase 9
Topics
  • Aged
  • Dihydrouracil Dehydrogenase (NADP)
  • Humans
  • Male
  • Matrix Metalloproteinase 9 (blood)
  • Middle Aged
  • Neoplasm Proteins (blood)
  • Oxidoreductases (analysis)
  • Pentosyltransferases (analysis)
  • Pyrimidine Phosphorylases
  • Stomach (enzymology)
  • Stomach Neoplasms (enzymology, pathology)

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