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http://purl.uniprot.org/citations/15238359http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15238359http://www.w3.org/2000/01/rdf-schema#comment"Maternofetal transport of l-carnitine, a molecule that shuttles long-chain fatty acids to the mitochondria for oxidation, is thought to be important in preparing the fetus for its lipid-rich postnatal milk diet. Using brush-border membrane (BBM) vesicles from human term placentas, we showed that l-carnitine uptake was sodium and temperature dependent, showed high affinity for carnitine (apparent K(m) = 11.09 +/- 1.32 microM; V(max) = 41.75 +/-0.94 pmol.mg protein(-1).min(-1)), and was unchanged over the pH range from 5.5 to 8.5. l-Carnitine uptake was inhibited in BBM vesicles by valproate, verapamil, tetraethylammonium, and pyrilamine and by structural analogs of l-carnitine, including d-carnitine, acetyl-d,l-carnitine, and propionyl-, butyryl-, octanoyl-, isovaleryl-, and palmitoyl-l-carnitine. Western blot analysis revealed that OCTN2, a high-affinity, Na(+)-dependent carnitine transporter, was present in placental BBM but not in isolated basal plasma membrane vesicles. The reported properties of OCTN2 resemble those observed for l-carnitine uptake in placental BBM vesicles, suggesting that OCTN2 may mediate most maternofetal carnitine transport in humans."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.org/dc/terms/identifier"doi:10.1152/ajpcell.00333.2003"xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/author"Qureshi I.A."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/author"Mitchell G.A."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/author"Lafond J."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/author"Lahjouji K."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/author"Leduc L."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/author"Elimrani I."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/name"Am J Physiol Cell Physiol"xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/pages"C263-9"xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/title"L-Carnitine transport in human placental brush-border membranes is mediated by the sodium-dependent organic cation transporter OCTN2."xsd:string
http://purl.uniprot.org/citations/15238359http://purl.uniprot.org/core/volume"287"xsd:string
http://purl.uniprot.org/citations/15238359http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15238359
http://purl.uniprot.org/citations/15238359http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15238359
http://purl.uniprot.org/uniprot/O76082#attribution-3F6DBC705AFE2FA0DCF6898B27D264B7http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15238359
http://purl.uniprot.org/uniprot/O76082#attribution-C23A2FB018AE4D6090A1E52F710D16E9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15238359
http://purl.uniprot.org/uniprot/#_O76082-mappedCitation-15238359http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15238359
http://purl.uniprot.org/uniprot/#_Q59FH6-mappedCitation-15238359http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15238359
http://purl.uniprot.org/uniprot/O76082http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15238359
http://purl.uniprot.org/uniprot/Q59FH6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15238359