3′-Azido-3′-deoxythymidine (AZT) is a competitive inhibitor of thymidine phosphorylation in isolated rat heart and liver mitochondria

Matthew D. Lynx, Edward E. McKee

Research output: Contribution to journalArticlepeer-review

60 Scopus citations

Abstract

Long-term use of 3′-azido-3′-deoxythymidine (AZT) is associated with various tissue toxicities, including hepatotoxicity and cardiomyopathy, and with mitochondrial DNA depletion. AZT-5′-triphosphate (AZTTP) is a known inhibitor of the mitochondrial DNA polymerase γ and has been targeted as the source of the mitochondrial DNA depletion. However, in previous work from this laboratory with isolated rat heart and liver mitochondria, AZT itself was shown to be a more potent inhibitor of thymidine phosphorylation (IC50 of 7.0 ± 1.0 μM AZT in heart mitochondria and of 14.4 ± 2.6 μM AZT in liver mitochondria) than AZTTP is of polymerase γ (IC50 of >100 μM AZTTP), suggesting that depletion of mitochondrial stores of TTP may limit replication and could be the cause of the mitochondrial DNA depletion observed in tissues affected by AZT toxicity. The purpose of this work is to characterize the nature of AZT inhibition of thymidine phosphorylation in isolated rat heart and rat liver mitochondria. In both of these tissues, AZT was found to be a competitive inhibitor of the phosphorylation of thymidine to TMP, catalyzed by thymidine kinase 2. The inhibition constant (Ki) for heart mitochondria is 10.6 ± 4.5 μM AZT, and for liver mitochondria Ki is 14.0 ± 2.5 μM AZT. Since AZT is functioning as a competitive inhibitor, increasing thymidine concentrations may be one mechanism to overcome the inhibition and decrease AZT-related toxicity in these tissues.

Original languageEnglish
Pages (from-to)239-243
Number of pages5
JournalBiochemical Pharmacology
Volume72
Issue number2
DOIs
StatePublished - Jul 14 2006

Keywords

  • AZT
  • Competitive inhibition
  • Mitochondrial toxicity
  • Nucleoside reverse transcriptase inhibitors (NRTIs)
  • Thymidine
  • Thymidine kinase 2

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