Xenobiotic metabolizing and antioxidant enzymes in normal and neoplastic human breast tissue

Eur J Drug Metab Pharmacokinet. Oct-Dec 1998;23(4):497-500. doi: 10.1007/BF03190001.

Abstract

An investigation was made of ethoxyresorufin O-deethylase (EROD) activity, a cytochrome P450 (CYP) dependent enzyme mainly catalyzed by CYP1A1, glutathione S-transferase (GST) activity toward the substrates 1-chloro-2,4- dinitrobenzene (CDNB) and ethacrynic acid (EAA), reduced glutathione (GSH) levels, and antioxidant enzyme (AOE) activity namely catalase (CAT) and selenium- dependent glutathione peroxidase (Se-GPx) in tumor and surrounding tumor-free (normal) tissues in female breast cancer patients. Wide interindividual variations were found in the enzyme activities in both tumor and normal breast tissues. No significant differences were noted between mean EROD and CAT activities in tumor and normal breast tissues. The mean activities of CDNB GST, EAA GST and Se-GPx and GSH levels in tumor tissue were significantly higher than those in normal breast tissue. These results show that CYP, GST and AOE behave differentially in breast tumors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antioxidants / metabolism
  • Breast / enzymology*
  • Breast Neoplasms / enzymology*
  • Catalase / metabolism
  • Cytochrome P-450 CYP1A1 / metabolism
  • Dinitrochlorobenzene / metabolism
  • Enzymes / metabolism*
  • Ethacrynic Acid / metabolism
  • Female
  • Glutathione Peroxidase / metabolism
  • Glutathione Transferase / metabolism
  • Humans
  • Selenium / physiology
  • Xenobiotics / metabolism

Substances

  • Antioxidants
  • Dinitrochlorobenzene
  • Enzymes
  • Xenobiotics
  • Catalase
  • Glutathione Peroxidase
  • Cytochrome P-450 CYP1A1
  • Glutathione Transferase
  • Selenium
  • Ethacrynic Acid