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• W2279657354 abstract "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 10−6M) produced a concentration-dependent inhibition of LPO, which was greatly decreased by polymyxin B (Px B) (an inhibitor of PK-C). The non-active analogue of PMA, 4α-phorbol-12,13-didecanoate (4α-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." @default.
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• W2279657354 date "1988-01-01" @default.
• W2279657354 modified "2023-09-27" @default.
• W2279657354 title "The Role of Secondary Messengers in the Regulation of Lipid Peroxidation in Rat Liver Microsomes" @default.
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• W2279657354 doi "https://doi.org/10.3109/10715768809066892" @default.
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