Molecular cloning and functional characterization of two alternatively spliced Ntcp isoforms from mouse liver1.
To isolate the murine Na+/taurocholate cotransporting polypeptide (Ntcp), we screened a mouse liver cDNA library and identified Ntcp1, encoding a 362 amino acid protein and Ntcp2, encoding a 317 amino acid protein which had a shorter C-terminal end. Both isoforms mediated saturable Na+-dependent transport of taurocholate when expressed in Xenopus laevis oocytes. Analysis of the gene revealed that Ntcp2 is produced by alternative splicing where the last intron is retained.
Cattori
V
V
Division of Clinical Pharmacology and Toxicology, Department of Medicine, University Hospital, CH-8091, Zurich, Switzerland.
Eckhardt
U
U
Hagenbuch
B
B
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D015723:Gene Library; D008099:Liver / Q000378:metabolism*; D026901:Membrane Transport Proteins; D051379:Mice; D008969:Molecular Sequence Data; D009865:Oocytes / Q000378:metabolism; D029363:Organic Anion Transporters, Sodium-Dependent; D020033:Protein Isoforms / Q000235:genetics; D016415:Sequence Alignment; D027981:Symporters; D014982:Xenopus laevis
D002352:Carrier Proteins; D026901:Membrane Transport Proteins; D029363:Organic Anion Transporters, Sodium-Dependent; D020033:Protein Isoforms; D027981:Symporters; C071908:sodium-bile acid cotransporter