High uridine phosphorylase activity in human melanoma tumor.
Uridine (Urd) phosphorylase and Urd kinase activities were examined in 4 human tumor types including melanoma and human and mouse melanoma cell lines. Urd phosphorylase activity in melanoma tumor specimens was higher than in specimens of colon, ovarian, and breast tumors. Urd kinase activity levels were similar in the 4 tumor types. In 3 human melanoma cell lines examined, Urd phosphorylase activity was markedly greater than in mouse B16 melanoma cells, while Urd kinase activity did not differ appreciably in the human and mouse cell lines. Urd phosphorylase activity in crude extract preparations from different melanoma cell lines showed similar substrate affinity and sensitivity to 1-(2'-deoxy-beta-D-glucopyranosyl)-thymine, a specific inhibitor. The high Urd phosphorylase activity found in melanoma tumor tissue may be exploited in the treatment of malignant melanoma with antipyrimidine agents. Cultured human melanoma cells retain this biochemical characteristic and may serve as appropriate in vitro models for the human tumor in studies concerning pyrimidine metabolism.
D000818:Animals; D001943:Breast Neoplasms / Q000201:enzymology; D002460:Cell Line; D003110:Colonic Neoplasms / Q000201:enzymology; D005260:Female; D006801:Humans; D007700:Kinetics; D008545:Melanoma / Q000201:enzymology*; D051379:Mice; D009369:Neoplasms / Q000201:enzymology*; D010051:Ovarian Neoplasms / Q000201:enzymology; D010430:Pentosyltransferases / Q000032:analysis*; D014541:Uridine Kinase / Q000032:analysis / Q000378:metabolism; D014543:Uridine Phosphorylase / Q000032:analysis* / Q000378:metabolism
D010430:Pentosyltransferases; D014543:Uridine Phosphorylase; D014541:Uridine Kinase