Role of microsomal ethanol-oxidizing system in regulation of linoleoyl-CoA desaturase activity after long-term ethanol administration.
Chronic ethanol administration resulted in a decrease of rat liver linoleoyl-CoA desaturase activity and an activation of MEOS. This was accompanied by an increase in the activity of the NADPH-dependent system and the oxidation rate of NADH-oxidase, which suggests transfer of electrons from NADH to cytochrome P-450. The decreased linoleoyl-CoA desaturase activity may be due to insufficient supply of electrons, because of possible diversion to MEOS.
Buko
V U
VU
Institute of Biochemistry, Byelorussian SSR Academy of Sciences, Grodno.
Sushko
L I
LI
D000818:Animals; D003579:Cytochrome Reductases / Q000378:metabolism; D042966:Cytochrome-B(5) Reductase; D000431:Ethanol / Q000378:metabolism*; D044943:Fatty Acid Desaturases / Q000378:metabolism*; D050602:Linoleoyl-CoA Desaturase; D008099:Liver / Q000201:enzymology*; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology / Q000502:physiology*; D009097:Multienzyme Complexes / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D010084:Oxidation-Reduction; D051381:Rats; D011919:Rats, Inbred Strains
D009097:Multienzyme Complexes; D000431:Ethanol; D044943:Fatty Acid Desaturases; D050602:Linoleoyl-CoA Desaturase; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; D003579:Cytochrome Reductases; D042966:Cytochrome-B(5) Reductase