Peroxisome proliferative drugs do not induce an increase of rat mevalonate pyrophosphate decarboxylase.
To determine whether or not the expression of mevalonate pyrophosphate decarboxylase (MPD) depends on the proliferation of peroxisomes, we examined change in the protein level of MPD in the crude extract, the cytosol and the peroxisome-enriched fraction of the livers of rats administered peroxisome proliferative drugs. No increase of MPD was observed in any of these fractions. These data suggest that the expression of MPD is independent of the proliferation of peroxisomes and may be maintained via a specific regulatory mechanism different from that of the expression of peroxisome proliferator-activated receptor alpha.
Michihara
Akihiro
A
Faculty of Pharmacy and Pharmaceutical Sciences, Fukuyama University, Gakuencho, Fukuyama, Hiroshima 729-0292, Japan. mitihara@fupharm.fukuyama-u.ac.jp
Sawamura
Makoto
M
Yamori
Yukio
Y
Akasaki
Kenji
K
Tsuji
Hiroshi
H
D000818:Animals; D002262:Carboxy-Lyases / Q000096:biosynthesis*; D002994:Clofibrate / Q000494:pharmacology; D003687:Dehydroepiandrosterone / Q000494:pharmacology; D004790:Enzyme Induction / Q000187:drug effects / Q000502:physiology; D008099:Liver / Q000187:drug effects / Q000201:enzymology; D008297:Male; D020675:Peroxisomes / Q000187:drug effects* / Q000201:enzymology*; D051381:Rats; D011921:Rats, Inbred WKY
D003687:Dehydroepiandrosterone; D002262:Carboxy-Lyases; C022503:pyrophosphomevalonate decarboxylase; D002994:Clofibrate