Functional interaction between peroxisome proliferator-activated receptors-alpha and Mef-2C on human carnitine palmitoyltransferase 1beta (CPT1beta) gene activation

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dc.contributor	Universitat de Barcelona
dc.contributor.author	Baldán Aranda, Ángel
dc.contributor.author	Relat Pardo, Joana
dc.contributor.author	Marrero González, Pedro F.
dc.contributor.author	Haro Bautista, Diego
dc.date	2013-11-28T16:03:17Z
dc.date	2013-11-28T16:03:17Z
dc.date	2004
dc.date	2013-11-28T16:03:17Z
dc.identifier.citation	0305-1048
dc.identifier.citation	527452
dc.identifier.uri	http://hdl.handle.net/2445/48163
dc.format	8 p.
dc.format	application/pdf
dc.language.iso	eng
dc.publisher	Oxford University Press
dc.relation	Reproducció del document publicat a: http://dx.doi.org/10.1093/nar/gkh806
dc.relation	Nucleic Acids Research, 2004, vol. 32, num. 16, p. 4742-4749
dc.relation	http://dx.doi.org/10.1093/nar/gkh806
dc.rights	cc-by-nc (c) Baldán Aranda, Ángel et al., 2004
dc.rights	info:eu-repo/semantics/openAccess
dc.rights	http://creativecommons.org/licenses/by-nc/3.0/es
dc.subject	Àcids grassos
dc.subject	Oxidació fisiològica
dc.subject	Receptors nuclears (Bioquímica)
dc.subject	Factors de transcripció
dc.subject	Transferases
dc.subject	Fatty acids
dc.subject	Physiological oxidation
dc.subject	Nuclear receptors (Biochemistry)
dc.subject	Transcription factors
dc.subject	Transferases
dc.title	Functional interaction between peroxisome proliferator-activated receptors-alpha and Mef-2C on human carnitine palmitoyltransferase 1beta (CPT1beta) gene activation
dc.type	info:eu-repo/semantics/article
dc.type	info:eu-repo/semantics/publishedVersion
dc.description.abstract	Muscle-type carnitine palmitoyltransferase 1 (CPT1β) is considered to be the gene that controls fatty acid mitochondrial β-oxidation. A functional peroxisome proliferator-activated receptor (PPAR) responsive element (PPRE) and a myocite-specific (MEF2) site that binds MEF2A and MEF2C in the promoter of this gene had been previously identified. We investigated the roles of the PPRE and the MEF2 binding sites and the potential interaction between PPARα and MEF2C regulating the CPT1β gene promoter. Mutation analysis indicated that the MEF2 site contributed to the activation of the CPT1β promoter by PPAR in C2C12 cells. The reporter construct containing the PPRE and the MEF2C site was synergistically activated by co-expression of PPAR, retinoid X receptor (RXR) and MEF2C in non-muscle cells. Moreover, protein-binding assays demonstrated that MEF2C and PPAR specifically bound to one another in vitro. Also for the synergistic activation of the CPT1β gene promoter by MEF2C and PPARα-RXRα, a precise arrangement of its binding sites was essential.

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