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• W1967025767 abstract "The competitive basis and specificity of deoxyuridylate (dUMP)-mediated decreases in thymidylate synthase-5'-fluorodeoxyuridylate-folate (TS-FdUMP-folate) ternary complex formation at low concentrations of folates were investigated using charcoal isolation of protein-bound [3H]FuUMP ligand. Reaction conditions used 0.02 μM TS (Lactobacillus casei) and 0.10 μM [3H]FdUMP incubated for 10 min at 37dg and pH 7.4. Decreases in counts below control (C) values in dUMP-added samples (S) were expressed as C/S ratios. At CH2-H2PteGlu1 or H4PteGlu1 concentrations below 10 μM, highly linear relationships were found to exist between C/S value and dUMP concentrations, expressed as dUMP/FdUMP ratios. For H4PteGlu1, maximal C/S values for dUMP interference occurred at the lowest H4PteGlu1 concentrations, approaching the value of the TS-FdUMP binary complex. The efficiency of ternary complex formation by H4PteGlu1 was 28 ± 5% of CH2-H4PteGlu1 values at concentrations below 1.0 μM. The protective effect of increasing H4PteGlu1 against dUMP interference resulted in a linear relationship between the logarithm of H4PteGlu1 concentration and the slope of dUMP interference (C/S vs dUMP/FdUMP). In contrast, the results with CH2-H4PteGlu1 were biphasic. At concentrations of CH2-H4PteGlu1 lower than 0.5 μM, C/S values were greater than those for binary complex alone, a result related to CH2-H4PteGlu1 consumption based on [5-3H]dUMP tritium-release studies. At concentrations of CH2-H4PteGlu1 above 1.0 μM, however, dUMP interference was nearly abolished. Kinetic analysis of the data suggests that this effect of the 5,10-methylene moiety may result in part from positive allosteric effects of first site TS-FdUMP-CH2-H4PteGlu1 ternary complex binding on acceleration of second site binding, in addition to slowed rates of dissociation. Other folylmonoglutamates showed relatively poor TS-[3H]FdUMP-folate complex formation: at 500 μM folate, as a percentage of CH2-H4PteGlu, values, these were 29.6% for dihydrofolate, 7.5% for 5-CH3-H4PteGlu1, 3.0% for CHH4PteGlu1, 1.6% for folic acid, 1.1% for 5-CHO-H4PteGlu1 (leucovorin) and 0.9% for 10-CHO-H4PteGlu,. Inhibitory effects by dUMP were consistent with binary complex effects alone for these folates. Study of methotrexate, as the monoglutamate and the hexaglutamate, suggested that ternary complexes with dUMP are favored over those with FdUMP at high concentrations of the antifolate. Our results indicate that activation of leucovorin to over 0.5 μM in intracellular CH2-H4PteGlu1 equivalents may be a requirement for achieving complete TS inhibition by FdUMP in the presence of excess concentrations of dUMP. Use of TS-[3H]FdUMP ligation to measure intracellular CH2-H4PteGlun concentrations may result in significant overestimates in the presence of excess H4PteGlun." @default.
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• W1967025767 date "1989-09-01" @default.
• W1967025767 modified "2023-10-16" @default.
• W1967025767 title "Deoxyuridylate effects on thymidylate synthase-5-fluorodeoxyuridylate-folate ternary complex formation" @default.
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• W1967025767 doi "https://doi.org/10.1016/0006-2952(89)90006-3" @default.
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