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Specific induction of lauric acid ω‐hydroxylase by clofibrate, diethylhexyl‐phthalate and 2,4‐dichlorophenoxyacetic acid in higher plants
Author(s) -
Salaün JeanPierre,
Simon Annick,
Durst Francis
Publication year - 1986
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02535411
Subject(s) - clofibrate , lauric acid , chemistry , hydroxylation , biochemistry , cinnamic acid , cytochrome p450 , cytochrome , phthalate , microsome , fatty acid , enzyme , organic chemistry
Recently, we have found in plant microsomes two laurate hydroxylases that catalyze the terminal hydroxylation or the in‐chain hydroxylation of the fatty acid. These two hydroxylases, which are both cytochrome P‐450 enzymes, are never found in the same plant. This study shows that the hypolipidemic drug clofibrate induces the lauric acid ω‐hydroxylase activity in Vicia and soybean seedlings. The marked increase in activity (>20‐fold) produced by clofibrate was dose‐dependent but was not paralleled by an enhancement of bulk cytochrome P‐450 or cinnamic acid 4‐hydroxylase. Compounds related to clofibrate by structure (2,4‐dichlorophenoxyacetic acid) or effects (diethylhexyl‐phthalate) also stimulated the ω‐hydroxylating system in these plants. In contrast, the lauric acid in‐chain hydroxylase from Jerusalem artichoke tubers was induced less than cinnamic acid 4‐hydroxylase activity and bulk cytochrome P‐450 in tissues incubated in clofibrate solution. This suggests that clofibrate induces preferentially the laurate ω‐hydroxylating isozyme in plants.