Literature summary for 1.14.14.80 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.

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Application

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

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
hepatocyte	cultured hepatocyte	Rattus norvegicus	-

Synonyms

Synonyms	Comment	Organism
CYP4A	-	Rattus norvegicus

Expression

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

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Release 2023.1 (January 2023)