Gi. Murray et al., THE IMMUNOHISTOCHEMICAL LOCALIZATION OF DRUG-METABOLIZING-ENZYMES IN PROSTATE-CANCER, Journal of pathology, 177(2), 1995, pp. 147-152
The major groups of enzymes involved in activating and detoxifying the
rapeutic drugs, not least several anti-cancer drugs, include the cytoc
hromes P350 (P450s), epoxide hydrolase, and glutathione S-transferases
(GSTs). The expression of these enzymes in malignant tumours is one p
ossible mechanism of anti-cancer drug resistance. This study has inves
tigated the presence, cellular localization, and distribution of drug-
metabolizing enzymes in prostate cancer. The P450 subfamilies CYP1A, C
YP2C, and CYP3A were present in 63, 25, and 61 per cent of tumours, re
spectively. Epoxide hydrolase was identified in 96 per cent of tumours
. GST-a and GST-mu were expressed in 29 and 41 per cent of tumours, re
spectively, while there was no immunoreactivity for the pi form of GST
. The absence of GST-pi in prostate cancer contrasts with the frequent
expression of GST-pi observed in other types of malignant tumour. In
non-neoplastic prostatic epithelium, there was expression of CYP1A, CY
P2C, epoxide hydrolase, and the different forms of GST, while there wa
s no apparent immunoreactivity for CYP3A.