Enzymic imbalance in serine metabolism in rat hepatomas
- 15 January 1986
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 233 (2) , 617-620
- https://doi.org/10.1042/bj2330617
Abstract
The activity of 3-phosphoglycerate dehydrogenase was high in tissues of high cell-renewal capacity, and was increased in neonatal and regenerating liver and, more markedly, in hepatomas. Serine hydroxymethyltransferase activity was present in hepatomas, whereas other enzymes of serine utilization (serine dehydratase and serine aminotransferase) were absent. This enzymic imbalance couples serine biosynthesis preferentially to nucleotide precursor formation in cancer cells.This publication has 12 references indexed in Scilit:
- Enzymes of serine metabolism in normal, developing and neoplastic rat tissuesAdvances in Enzyme Regulation, 1984
- Biochemical strategy of cancer cells and the design of chemotherapy: G. H. A. Clowes Memorial Lecture.1983
- The role of serine hydroxymethyltransferase in cell proliferation: DNA synthesis from serine following mitogenic stimulation of lymphocytesBioscience Reports, 1981
- Liver enzymes of serine metabolism during neonatal development of the ratBiochemical Journal, 1980
- Control of gene expression in carbohydrate, pyrimidine and DNA metabolismAdvances in Enzyme Regulation, 1971
- Two enzymes of serine metabolism in rat liver and hepatomas.1970
- Phosphoserine phosphatase distribution in normal and neoplastic rat tissuesArchives of Biochemistry and Biophysics, 1969
- The Biosynthesis of Serine in Mouse Brain ExtractsJournal of Biological Chemistry, 1965
- Purification and Properties of Chicken Liver D-3-Phosphoglycerate Dehydrogenase*Biochemistry, 1965
- Enzymology and Regulation of Serine Biosynthesis in Cultured Human CellsJournal of Biological Chemistry, 1964