Pyrimidine metabolism in peripheral and phytohemagglutinin-stimulated mammalian lymphocytes.
Abstract: 1. Activity of uridine kinase was very low in ovine lymphocytes and in those of some pigs. Lymphocytes of other pigs showed a significantly higher activity of this enzyme. Activity of uridine kinase in lymphocytes of man, horse and cattle was intermediate. 2. Activity of uridine phosphorylase was higher than that of uridine kinase with lymphocytes of all species. 3. Activity of uridine kinase in equine lymphocytes increases at PHA-stimulation and also in porcine lymphocytes with a low activity at the start of the culture. Activity of uridine kinase decreased in porcine lymphocytes with a high activity at the start of the culture. 4. Activity of uridine phosphorylase increases at PHA-stimulation with equine and porcine lymphocytes and during culturing of non-stimulated porcine lymphocytes. 5. Activities of OPRT and ODC decrease in cultures of porcine lymphocytes with and without PHA. 6. Activity of OPRT in lysates of porcine lymphocytes is inhibited by purine nucleosides and by guanine and pyrimidine nucleotides.
Publication Date: 1983-01-01 PubMed ID: 6825903DOI: 10.1016/0020-711x(83)90010-1Google Scholar: Lookup
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- Journal Article
Summary
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The research explores the activity of key enzymes involved in pyrimidine metabolism in mammalian lymphocytes. It investigates how these activities can vary among different species and can be influenced by PHA-stimulation and other factors.
Exploring Enzyme Activity Across Different Animal Species
- The research highlights that uridine kinase, an enzyme involved in the metabolism of the pyrimidine nucleoside uridine, has varying levels of activity across different animals. The lowest activity level was noted in ovine (sheep) lymphocytes and in some pigs. Enhanced activity was seen in other pigs. Intermediate activity was observed in the lymphocytes of humans, horses, and cattle.
- The activity of another enzyme, uridine phosphorylase, which is also involved in uridine metabolism, was higher than that of uridine kinase in lymphocytes of all tested species.
Response to PHA-Stimulation and Other Influences
- PHA, or phytohemagglutinin, is known to stimulate lymphocyte cell division and activity. The researchers found that it also affects the activity of enzymes in these cells. For instance, uridine kinase activity in horse and certain pig lymphocytes increased following PHA-stimulation. In contrast, this activity decreased in those pig lymphocytes that initially had high activity levels.
- Uridine phosphorylase activity also increased in response to PHA-stimulation in lymphocytes from horses and pigs. Non-stimulated pig lymphocytes also showed increased activity during culturing.
- Two other enzymes scrutinized in this study, OPRT (orotate phosphoribosyltransferase) and ODC (ornithine decarboxylase), both crucial for nucleotide synthesis, showed decreased activity levels in cultured pig lymphocytes, regardless of whether or not they were PHA-stimulated.
- Notably, the activity of OPRT in pig lymphocytes lysates was inhibited by the presence of both purine nucleosides (a type of nucleotide building block) and by guanine and pyrimidine nucleotides (the building blocks of DNA and RNA).
In conclusion, the study provides valuable insights into how pyrimidine metabolism may vary across different mammalian species, as well as how it can be influenced by stimulation and inhibition factors. These findings could have implications for our understanding of cellular metabolism and potentially the treatment of related diseases.
Cite This Article
APA
Peters GJ, Oosterhof A, Veerkamp JH.
(1983).
Pyrimidine metabolism in peripheral and phytohemagglutinin-stimulated mammalian lymphocytes.
Int J Biochem, 15(1), 51-55.
https://doi.org/10.1016/0020-711x(83)90010-1 Publication
Researcher Affiliations
MeSH Terms
- Adult
- Animals
- Cattle
- Horses
- Humans
- In Vitro Techniques
- Lymphocytes / enzymology
- Lymphocytes / metabolism
- Phytohemagglutinins / pharmacology
- Pyrimidine Nucleotides / metabolism
- Sheep
- Species Specificity
- Swine
- Uridine Kinase / metabolism
- Uridine Phosphorylase / metabolism
Citations
This article has been cited 1 times.- Peters GJ, Smid K, Vecchi L, Kathmann I, Sarkisjan D, Honeywell RJ, Losekoot N, Ohne O, Orbach A, Blaugrund E, Jeong LS, Lee YB, Ahn CH, Kim DJ. Metabolism, mechanism of action and sensitivity profile of fluorocyclopentenylcytosine (RX-3117; TV-1360). Invest New Drugs 2013 Dec;31(6):1444-57.
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