Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.7 (DNA polymerase)
 17,007 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The polyoxotungstate HPA-23 was found to exert a differential effect on the induction of Epstein-Barr virus early antigen in Raji cells induced with 5-iodo-2'-deoxyuridine (IUdR). Thus, treatment of Raji cells concomitantly with IUdR and HPA-23 inhibited early antigen expression, and the extent of inhibition was proportional to the duration of treatment with HPA-23. In contrast, pretreatment of Raji cells with HPA-23 prior to induction with IUdR stimulated early antigen expression in exponentially multiplying but not in stationary-phase cells. HPA-23 alone had no effect on early antigen expression in Raji cells. Activation of the latent Epstein-Barr virus genome by IUdR is dependent upon incorporation of the thymidine analogue into cellular DNA during the S-phase of the cell cycle. Synthesis of Epstein-Barr virus DNA also takes place during S-phase, suggesting a possible participation in this process of cellular DNA polymerase alpha which is thought to be responsible for cellular DNA replication and the activity of which increases several-fold during S-phase. Treatment of Raji cells with HPA-23 caused a marked decrease in DNA polymerase alpha activity, which could result in an inhibition of IUdR incorporation leading to the observed reduction of early antigen expression in cells treated concomitantly with IUdR and HPA-23.
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PMID:Modulation by the polyoxotungstate HPA-23 of Epstein-Barr virus early antigen expression in Raji cells treated with iododeoxyuridine. 632 25

Wheat germ DNA polymerase A, a gamma-like enzyme, recognized efficiently natural and synthetic RNA templates, resembling a retroviral reverse transcriptase (P. Laquel et al., Biochim Biophys Acta 1048 (1990): 139-148). Ammonium-21-tungsto-9-antimoniate (HPA-23), an antiviral drug, inhibited the DNA polymerase A activities, independently of the template primers used, i.e. activated DNA or polyriboadenylic acid oligodeoxythymidylate (poly(rA)-oligo(dT)). The inhibition observed in the poly(rA)-oligo(dT)-directed DNA polymerase A activity occurred in the presence of either Mg2+ or Mn2+ as divalent cation, and also with the 2'-fluoro analogue of poly(rA) as template. HPA-23 was a non-competitive inhibitor with respect to TTP, activated DNA, poly(rA)-oligo(dT), and poly(dAfl)-oligo(dT). A preincubation study showed a reversible HPA-23 binding to DNA polymerase A, in the presence of poly(rA)-oligo(dT) as the template primer.
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PMID:Inhibition of the wheat germ DNA polymerase A activity by the antiviral drug HPA-23. 826 Jun 25