Metabolism and bioactivation of famitinib, a novel inhibitor of receptor tyrosine kinase, in cancer patients

Br J Pharmacol. 2013 Apr;168(7):1687-706. doi: 10.1111/bph.12047.

Abstract

Background and purpose: Famitinib is a novel multi-targeted receptor tyrosine kinase inhibitor under development for cancer treatment. This study aims to characterize the metabolic and bioactivation pathways of famitinib.

Experimental approach: The metabolites in human plasma, urine and feces were identified via ultra-high performance liquid chromatography-quadrupole-time of flight-mass spectrometry and confirmed using synthetic standards. Biotransformation and bioactivation mechanisms were investigated using microsomes, recombinant metabolic enzymes and hepatocytes.

Key results: Famitinib was extensively metabolized after repeated oral administrations. Unchanged famitinib was the major circulating material, followed by N-desethylfaminitib (M3), whose steady-state exposure represented 7.2 to 7.5% that of the parent drug. Metabolites in the excreta were mainly from oxidative deamination (M1), N-desethylation (M3), oxidative defluorination (M7), indolylidene hydroxylation (M9-1 and M9-5) and secondary phase-II conjugations. CYP3A4/5 was the major contributor to M3 formation, CYP3A4/5 and aldehyde dehydrogenase to M1 formation and CYP1A1/2 to M7, M9-1 and M9-5 formations. Minor cysteine conjugates were observed in the plasma, urine and feces, implying the formation of reactive intermediate(s). In vitro microsomal studies proved that famitinib was bioactivated through epoxidation at indolylidene by CYP1A1/2 and spontaneously defluorinated rearrangement to afford a quinone-imine species. A correlation between famitinib hepatotoxicity and its bioactivation was observed in the primary human hepatocytes.

Conclusion and implications: Famitinib is well absorbed and extensively metabolized in cancer patients. Multiple enzymes, mainly CYP3A4/5 and CYP1A1/2, are involved in famitinib metabolic clearance. The quinone-imine intermediate formed through bioactivation may be associated with famitinib hepatotoxicity. Co-administered CYP1A1/2 inducers or inhibitors may potentiate or suppress its hepatotoxicity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Administration, Oral
  • Adult
  • Antineoplastic Agents / metabolism
  • Antineoplastic Agents / pharmacokinetics*
  • Biotransformation
  • Cytochrome P-450 Enzyme System / metabolism
  • Female
  • Hepatocytes / drug effects
  • Hepatocytes / metabolism
  • Humans
  • Indoles / metabolism
  • Indoles / pharmacokinetics*
  • Isoenzymes / metabolism
  • Male
  • Microsomes, Liver / metabolism
  • Middle Aged
  • Neoplasms / metabolism*
  • Oxidation-Reduction
  • Pyrroles / metabolism
  • Pyrroles / pharmacokinetics*
  • Receptor Protein-Tyrosine Kinases / antagonists & inhibitors*
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Tissue Distribution

Substances

  • Antineoplastic Agents
  • Indoles
  • Isoenzymes
  • Pyrroles
  • famitinib
  • Cytochrome P-450 Enzyme System
  • Receptor Protein-Tyrosine Kinases