Deoxycytidylate aminohydrolase activity in the Novikoff hepatoma is dependent on the localization of the tumor.
The activity of deoxycytidylate aminohydrolase, a pivotal enzyme for pyrimidine biosynthesis in mammalian tissue, is 100x greater in the Novikoff hepatoma harvested from the intraperitoneal cavity than in the same tumor excised from either subcutaneous or intramuscular sites. The increased enzyme activity in the intraperitoneal tumor is not due to an increase in protein synthesis, since there are no significant differences in enzyme activity between normal liver, and either the subcutaneous or intramuscular hepatomas. Evidence is presented which indicates that deoxycytidylate aminohydrolase activity, and the expression of alternate pathways of pyrimidine biosynthesis in the Novikoff hepatoma, is dependent on the localization of the tumor within the host.
Sheid
B
B
Department of Pharmacology, State University of New York, Brooklyn.
D000818:Animals; D003844:DCMP Deaminase / Q000032:analysis*; D003856:Deoxyuracil Nucleotides / Q000096:biosynthesis; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D009709:Nucleotide Deaminases / Q000032:analysis*; D009928:Organ Specificity; D051381:Rats; D011919:Rats, Inbred Strains
D003856:Deoxyuracil Nucleotides; C007267:2'-deoxyuridylic acid; D009709:Nucleotide Deaminases; D003844:DCMP Deaminase