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- W122640819 abstract "A clofibrate inducible P450 that carries out the ω and ω-1 oxidation of fatty acids was purified from liver [1,2] and antibody derived from the purified protein was used to isolate a cDNA [1]. The “clofibrate-inducible” rat P450 was later named CYP4A1 based on the nomenclature system developed for the P450 superfamily (http://drnelson.utmem.edu/CytochromeP450.html). Two additional members of the CYP4A family were found in rats [3,4]. The CYP4A1 was the first member of a subfamily of P450s that oxidize a number of endogenous and exogenous fatty acids. Treatment of rats with clofibrate results in a rapid induction of CYP4A1 gene transcription and mRNA [2]. The mechanism of induction by clofibrate remained elusive until the discovery of the peroxisome proliferator-activated receptor (PPAR) in 1990 [5,6]. This receptor, subsequently named PPARα, is one of three members of a family in the nuclear receptor superfamily. The CYP4A1 gene was found to possess a functional binding site for PPARα [7]. Two additional members of the PPAR family were subsequently discovered and named PPARβ(δ) and PPARγ [8,9]. Only PPARα is able to induce transcription of the CYP4A P450s in liver and kidney of species that are responsive to peroxisome proliferators. The PPARs are representative of a group of nuclear receptors that require retinoid X receptor (RXR) as an obligate heterodimeric partner for activity [10]." @default.
- W122640819 created "2016-06-24" @default.
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- W122640819 date "2002-01-01" @default.
- W122640819 modified "2023-09-26" @default.
- W122640819 title "The Role of PPARα in Fatty Acid Metabolism and Hepatocarcinogenesis: Studies with PPARα-Null Mice" @default.
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- W122640819 doi "https://doi.org/10.1007/978-1-4615-1171-7_9" @default.
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