Structure-activity relationships of chlorinated benzenes as inducers of different forms of cytochrome P-450 in rat liver |
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| Authors: | JA Goldstein P Linko JN Huckins DL Stalling |
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| Institution: | 1. National Institute of Environmental Health Sciences, P.O. Box 12233, Research Triangle Park, NC 27709 U.S.A.;2. United States Department of the Interior, Fish and Wildlife Service, Columbia National Fishery Research Laboratory, Columbia, MO 65201 U.S.A. |
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| Abstract: | Hexachlorobenzene (HCB) produced increases in ethoxyresorufin (ERR) O-deethylase, aryl hydrocarbon hydroxylase (AHH) and aminopyrine N-demethylase activities in rat liver microsomes which were intermediate between those produced by phenobarbital and 3,4-benzpyrene (BP). α-Naphthoflavone (ANF) selectively inhibited ERR activity in BP and HCB-induced microsomes (94% and 88%). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of liver microsomes indicated that HCB did not produce a detectable increase in a polypeptide with electrophoretic properties similar to those of purified cytochrome P-448 (Mr = 56 000). However, HCB did induce a polypeptide with Mr = 53 000 corresponding to one of two polypeptide bands induced by BP. This polypeptide may represent a second form of cytochrome P-448. Purification of HCB to remove possible dibenzo-p-dioxin impurities did not alter the ‘mixed-type’ induction produced by HCB. In contrast to HCB, all other chlorinated benzenes tested resembled phenobarbital as inducers. |
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| Keywords: | AHH aryl hydrocarbon hydroxylase ANF α-naphthoflavone BP 3 4-benzpyrene ERR ethoxyresorufin ETNC ethyl isocyanide HCB hexachlorobenzene 3-MC 3-methylcholanthrene SDS-PAGE sodium dodecyl sulfate-polyacrylamide gel electrophoresis TCDD |
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