Cytochrome P-450 refers to a family of heme proteins present in mammalian cells as well as in plants and prokaryotes. Substrates for mammalian P-450 enzymes (P-450s) comprise endogenously synthesized compounds as well as xenobiotic compounds including medicines, food additives and environmental pollutants. There are many various isoforms of P450s, which have overlapping but distinct substrate specificities.

Although the total level of liver microsomal P450s does not vary considerably among humans, genetic polymorphism and inducibility of a given P-450 isoenzymes gives the interindividual variations in the levels of P450 isoforms (CYPs). What is more, the variability in expression of CYPs was observed between various tissues and between tumor and normal cells. Such differences indicate the opportunities for the development of prodrugs, which are nontoxic to normal cells and are activated to cytotoxic agents only within the tumor tissue. Gene directed therapy may be also included in this respect. On the other hand, P-450s are capable of deactivating of anticancer drugs, thus, inhibitors of the specific isoenzymes in tumor cells would be developed as modulators of antitumor activity.

Considering all above, studies on metabolic transformations of antitumor agents are concentrated on their susceptibility to transformation with individual forms of cytochrome P-450. There was reported earlier that cyclophosphamide was metabolized by CYP2B6, whereas transformation of tamoxifen occurred with CYP3A7 and CYP3A5 giving rise different products in each case.

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