Sodium-dependent carnitine transport in human placental choriocarcinoma cells

• Published in: Biochimica et biophysica acta Vol. 1284; no. 1; pp. 109 - 117
• Main Authors: Prasad, Puttur D., Huang, Wei, Ramamoorthy, Sammanda, Carter, A.Lee, Leibach, Frederick H., Ganapathy, Vadivel
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 02.10.1996
• Subjects: Binding Sites; Biological Transport; Carnitine; Carnitine - metabolism; Cell Membrane - metabolism; Choriocarcinoma - metabolism; Female; High-affinity binding; High-affinity transport; Human placenta; Humans; JAR choriocarcinoma cell; Placenta - metabolism; Plasma membrane; Pregnancy; Sodium - metabolism; Tumor Cells, Cultured; Uterine Neoplasms - metabolism; Human placenta; High-affinity transport; High-affinity binding; Plasma membrane; Carnitine; JAR choriocarcinoma cell
• ISSN: 0005-2736; 0006-3002; 1879-2642
• DOI: 10.1016/0005-2736(96)00126-5

The JAR human placental choriocarcinoma cells were found to transport carnitine into the intracellular space by a Na +-dependent process. The transport showed no requirement for anions. The Na +-dependent process was saturable and the apparent Michaelis-Menten constant for carnitine was 12.3 ± 0.5 μM. Na + activated the transport by increasing the affinity of the transport system for carnitine. The transport system specifically interacted with l-carnitine, d-carnitine, acetyl- dl-carnitine and betaine. 6- N-Trimethyllysine and choline had little or no effect on carnitine transport. Of the total transport measured, transport into the intracellular space represented 90%. Plasma membrane vesicles prepared from JAR cells were found to bind carnitine in a Na +-dependent manner. The binding was saturable with an apparent dissociation constant of 0.66 ± 0.08 μM. The binding process was specific for l-carnitine, d-carnitine, acetyl- dl-carnitine, and betaine, 6- N-Trimethyllysine and choline showed little or no affinity. It is concluded that the JAR cells express a Na +-dependent high-affinity system for carnitine transport and that the Na +-dependent high-affinity carnitine binding detected in purified JAR cell plasma membrane vesicles is possibly related to the transmembrane transport process.