Any feedback?
Please rate this page

BRENDA support

Literature summary for extracted from

  • Gatica, A.; Aguilera, M.C.; Contador, D.; Loyola, G.; Pinto, C.O.; Amigo, L.; Tichauer, J.E.; Zanlungo, S.; Bronfman, M.
    P450 CYP2C epoxygenase and CYP4A omega-hydroxylase mediate ciprofibrate-induced PPARalpha-dependent peroxisomal proliferation (2007), J. Lipid Res., 48, 924-934.
    View publication on PubMed


Application Comment Organism
medicine specific inhibition of either the CYP2C epoxygenase or the CYP4A omega-hydroxylase abrogates peroxisomal proliferation induced by the hypolipidemic drug cirpofibrate Rattus norvegicus


Organism UniProt Comment Textmining
Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
hepatocyte cultured hepatocyte Rattus norvegicus


Synonyms Comment Organism
Rattus norvegicus


Organism Comment Expression
Rattus norvegicus in ciprofibrate-treated cells, CYP4A expression increases by 1.5- to 1.8fold up

General Information

General Information Comment Organism
physiological function omega-hydroxylated eicosatrienoic acids may serve as endogenous peroxisome proliferator-activated receptor alpha ligands. P450 arachidonic acid monooxygenases such as CYP2C epoxygenase and CYP4A omega-hydroxylase participate in ciprofibrate-induced peroxisomal proliferation and the activation of peroxisome proliferator-activated receptor alpha downstream targets Rattus norvegicus