Enzymatic mechanism of the tumoricidal action of 4-iodo-3-nitrobenzamide.

doi:10.3892/mmr_00000165

Paper

Enzymatic mechanism of the tumoricidal action of 4-iodo-3-nitrobenzamide.

Published Sep 1, 2009 · E. Kun, J. Mendeleyev, A. Hakam

Molecular medicine reports

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9

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Abstract

Activation of the prodrug 4-iodo-3-nitrobenzamide critically depends on the cellular reducing system specific to cancer cells. In non-malignant cells, reduction of this prodrug to the non-toxic amine occurs by the flavoprotein of complex?I of mitochondria receiving Mg2+-ATP-dependent reducing equivalents from NADH to NADPH via pyridine nucleotide transhydrogenation. This hydride transfer is deficient in malignant cells; therefore, the lethal synthesis of 4-iodo-3-nitrosobenzamide takes place selectively. Enzymatic evidence for this mechanism has been provided by cellular studies with lysolecithin-permeabilized cells and cell fractions, which have identified the defect in transhydrogenation in neoplastic cells to be located at the energy transfer site. Confirming previous results, the present study demonstrates the validity of the selective tumoricidal action of the prodrug in cell cultures.

Study Snapshot

The selective tumoricidal action of 4-iodo-3-nitrobenzamide in cancer cells is due to a defect in hydride transfer at the energy transfer site.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Enzymatic mechanism of the tumoricidal action of 4-iodo-3-nitrobenzamide.

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