Title: Pyrimidine Metabolism in Folate Deficient Lymphoblasts
Abstract: Thymidine kinase (EC 2.7.1.2), the initial enzyme of the pyrimidine salvage pathway, catalyzes the phosphorylation of thymidine to thymidine monophosphate (1). Although increases in thymidine kinase activity parallel corresponding changes in cellular DNA synthesis (2–4), the exact mechanisms for control of this activity are ill understood. Of some relevance, in this regard, has been the increased thymidine kinase activities occurring in either dormant (5) or proliferating human folate deficient lymphocytes (6) with the augmented activity under these circumstances postulated to reflect enzyme induction secondary to a presumed reduced thymidylate pool (5,6). Recently we have developed an in vitro system for the production of folate deficiency in human lymphoblasts by mitogen stimulation of peripheral blood lymphocytes in folate restricted RPMI 1640 medium (7). The changes of thymidine kinase activities in relationship to controlled fluctuations of the cellular thymidine triphosphate pool in this system are reported here.
Publication Year: 1984
Publication Date: 1984-01-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 1
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