Inhibition of ferrochelatase by N-methylprotoporphyrin IX is not accompanied by delta-aminolevulinic acid synthetase induction in chick embryo liver cell culture.
N-Methylprotoporphyrin has been shown to markedly inhibit ferrochelatase activity in chick embryo liver cell culture without inducing delta-aminolevulinic acid (ALA) synthetase activity. This result supports the idea that the effects of 3,5-diethoxycarbonyl-1,4-dihydro-2,4,6-trimethylpyridine (DDC) on ALA synthetase activity and ferrochelatase activity are dissociated and that inhibition of ferrochelatase alone is not sufficient to cause induction of ALA synthetase. We conclude that the porphyrinogenic activity of DDC can be explained only in part by the actions of N-methylprotoporphyrin.
D000624:5-Aminolevulinate Synthetase / Q000096:biosynthesis*; D000818:Animals; D002478:Cells, Cultured; D002642:Chick Embryo; D004790:Enzyme Induction / Q000187:drug effects; D005294:Ferrochelatase / Q000037:antagonists & inhibitors*; D008099:Liver / Q000201:enzymology; D008190:Lyases / Q000037:antagonists & inhibitors*; D011166:Porphyrins / Q000378:metabolism / Q000494:pharmacology*; D011524:Protoporphyrins / Q000494:pharmacology*
D011166:Porphyrins; D011524:Protoporphyrins; C028842:N-methylprotoporphyrin IX; D000624:5-Aminolevulinate Synthetase; D008190:Lyases; D005294:Ferrochelatase