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dc.contributor.authorSierra, Adriana Y.
dc.contributor.authorGratacòs-Batlle, Esther
dc.contributor.authorCarrasco, Patricia
dc.contributor.authorClotet Erra, Josep
dc.contributor.authorUreña, Jesús
dc.contributor.authorSerra, Dolors
dc.contributor.authorAsins, Guillermina
dc.contributor.authorHegardt, Fausto G.
dc.contributor.authorCasals i Farré, Núria
dc.date.accessioned2020-07-07T12:01:30Z
dc.date.available2020-07-07T12:01:30Z
dc.date.issued2008
dc.identifier.citationSierra, Adriana Y.; Gratacós, Esther; Carrasco, Patricia [et al.]. CPT1c is localized in endoplasmic reticulum of neurons and has carnitine palmitoyltransferase activity. Journal of Biological Chemistry, 2008. 283, p. 6878-6885. Disponible en: <https://www.jbc.org/content/283/11/6878>. Fecha de acceso: 7 jul. 2020. DOI: 10.1074/jbc.M707965200ca
dc.identifier.issn1083-351Xca
dc.identifier.urihttp://hdl.handle.net/20.500.12328/1620
dc.description.abstractCPT1c is a carnitine palmitoyltransferase 1 (CPT1) isoform that is expressed only in the brain. The enzyme has recently been localized in neuron mitochondria. Although it has high sequence identity with the other two CPT1 isoenzymes (a and b), no CPT activity has been detected to date. Our results indicate that CPT1c is expressed in neurons but not in astrocytes of mouse brain sections. Overexpression of CPT1c fused to the green fluorescent protein in cultured cells demonstrates that CPT1c is localized in the endoplasmic reticulum rather than mitochondria and that the N-terminal region of CPT1c is responsible for endoplasmic reticulum protein localization. Western blot experiments with cell fractions from adult mouse brain corroborate these results. In addition, overexpression studies demonstrate that CPT1c does not participate in mitochondrial fatty acid oxidation, as would be expected from its subcellular localization. To identify the substrate of CPT1c enzyme, rat cDNA was overexpressed in neuronal PC-12 cells, and the levels of acylcarnitines were measured by high-performance liquid chromatography-mass spectrometry. Palmitoylcarnitine was the only acylcarnitine to increase in transfected cells, which indicates that palmitoyl-CoA is the enzyme substrate and that CPT1c has CPT1 activity. Microsomal fractions of PC-12 and HEK293T cells overexpressing CPT1c protein showed a significant increase in CPT1 activity of 0.57 and 0.13 nmol·mg-1·min-1, respectively, which is ∼50% higher than endogenous CPT1 activity. Kinetic studies demonstrate that CPT1c has similar affinity to CPT1a for both substrates but 20–300 times lower catalytic efficiency.ca
dc.format.extent23ca
dc.language.isoengca
dc.publisherAmerican Society for Biochemistry and Molecular Biologyca
dc.relation.ispartofJournal of Biological Chemistryca
dc.relation.ispartofseries283;
dc.rights© 2020 American Society for Biochemistry and Molecular Biologyca
dc.subject.otherCervell
dc.subject.otherMitocondris
dc.subject.otherNeurones
dc.subject.otherIsoenzims
dc.subject.otherCerebro
dc.subject.otherMitocondrias
dc.subject.otherNeuronas
dc.subject.otherIsoenzimas
dc.subject.otherBrain
dc.subject.otherMitochondria
dc.subject.otherNeurons
dc.subject.otherIsoenzymes
dc.titleCPT1c is localized in endoplasmic reticulum of neurons and has carnitine palmitoyltransferase activityca
dc.typeinfo:eu-repo/semantics/articleca
dc.description.versioninfo:eu-repo/semantics/acceptedVersionca
dc.embargo.termscapca
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/1PN/SAF2004-06843-C03ca
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/2PN/SAF2007-61926ca
dc.subject.udc61ca
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M707965200ca


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