The role of secondary messengers in the regulation of lipid peroxidation in rat liver microsomes.
The effect of phorbol-12-myristate-13-acetate (PMA), an activator of protein kinase C (PK-C) on lipid peroxidation (LPO) in rat liver homogenates and microsomes was studied. PMA (10(-10) to 10(-6) M) produced a concentration-dependent inhibition of LPO, which was greatly decreased by polymyxin B (PxB) (an inhibitor of PK-C). The non-active analogue of PMA, 4 alpha-phorbol-12,13-didecanoate (4 alpha-PDD) exerted no inhibitory effect. The adenylate cyclase activator, forskolin (FK) (10(-6) M) abolished the inhibitory effect of PMA on LPO. PMA and FK did not inhibit LPO in liposomes. It is suggested that LPO in biomembranes could be regulated by PK-C, whose inhibitory effect might be prevented by cAMP-dependent protein kinases.
Baldenkov
G N
GN
National Research Center for Cardiology, Academy of Medical Sciences USSR, Moscow.
Serbinova
E A
EA
Bakalova
R A
RA
Tkachuk
V A
VA
Kagan
V E
VE
Stoytchev
Ts S
TsS
D000818:Animals; D005576:Colforsin / Q000494:pharmacology; D015227:Lipid Peroxidation / Q000187:drug effects*; D008099:Liver / Q000378:metabolism*; D008297:Male; D008862:Microsomes, Liver / Q000378:metabolism*; D011112:Polymyxin B / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D015290:Second Messenger Systems; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D005576:Colforsin; D011112:Polymyxin B; D013755:Tetradecanoylphorbol Acetate