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Research Article Free access | 10.1172/JCI117091

Molecular cloning, chromosomal localization, and functional characterization of a human liver Na+/bile acid cotransporter.

B Hagenbuch and P J Meier

Department of Medicine, University Hospital, Zürich, Switzerland.

Find articles by Hagenbuch, B. in: PubMed | Google Scholar

Department of Medicine, University Hospital, Zürich, Switzerland.

Find articles by Meier, P. in: PubMed | Google Scholar

Published March 1, 1994 - More info

Published in Volume 93, Issue 3 on March 1, 1994
J Clin Invest. 1994;93(3):1326–1331. https://doi.org/10.1172/JCI117091.
© 1994 The American Society for Clinical Investigation
Published March 1, 1994 - Version history
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Abstract

We have used a cDNA probe from a cloned rat liver Na+/taurocholate cotransporting polypeptide (Ntcp) to screen a human liver cDNA library. A 1,599-bp cDNA clone that encodes a human Na+/taurocholate cotransporting polypeptide (NTCP) was isolated. The human NTCP consists of 349 amino acids (calculated molecular mass of 38 kD) and exhibits 77% amino acid homology with the rat Ntcp. In vitro translation experiments indicate that the protein is glycosylated and has a molecular weight similar to the rat Ntcp. Injection of in vitro transcribed cRNA into Xenopus laevis oocytes resulted in the expression of Na(+)-dependent taurocholate uptake. Saturation kinetics indicated that the human NTCP has a higher affinity for taurocholate (apparent Km = 6 microM) than the previously cloned rat protein (apparent Km = 25 microM). NTCP-mediated taurocholate uptake into oocytes was inhibited by all major bile acid derivatives (100 microM), bumetanide (500 microM), and bromosulphophthalein (100 microM). Southern blot analysis of genomic DNA from a panel of human/hamster somatic cell hybrids mapped the human NTCP gene to chromosome 14.

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