Effects of carbonyl compounds (4-hydroxyalkenals) originating from the peroxidation of liver microsomal lipids on various microsomal enzyme activities of the liver.
Carbonyl compounds released during the NADPH-Fe dependent peroxidation of liver microsomal lipids and identified as 4-hydroxyalkenals (almost entirely as 4-hydroxynonenal) while inhibiting microsomal enzymes (such as glucose 6-phosphatase and aminopyrine demethylase) which are affected by lipid peroxidation, have no effect on microsomal NADPH-cytochrome c reductase. The latter enzyme activity is unaffected (or even increased) when liver microsomes are allowed to peroxidize in the NADPH-Fe dependent system. NADPH-cytochrome c reductase, contrary to the other enzymes, is similarly unaffected after CCl4 poisoning, that is in a situation in which peroxidation of membrane lipids of liver endoplasmic reticulum has been unequivocally demonstrated. It appears therefore that the effects exherted by lipid peroxidation or by 4-hydroxyalkenals originating from lipid peroxidation parallel the effects of CCl4 intoxication in vivo.
D000447:Aldehydes / Q000378:metabolism / Q000494:pharmacology*; D000633:Aminopyrine N-Demethylase / Q000378:metabolism; D000818:Animals; D002252:Carbon Tetrachloride Poisoning / Q000378:metabolism; D005952:Glucose-6-Phosphatase / Q000378:metabolism; D066298:In Vitro Techniques; D008054:Lipid Peroxides / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D051381:Rats
D000447:Aldehydes; D008054:Lipid Peroxides; D000633:Aminopyrine N-Demethylase; D009251:NADPH-Ferrihemoprotein Reductase; D005952:Glucose-6-Phosphatase