{'fraction_non_alphanumeric': 0.029551954242135366, 'fraction_numerical': 0.02669208770257388, 'mean_word_length': 5.325301204819277, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
The voltage‐driven organic anion transport of type I sodium‐phosphate cotransporter and OATv1

Type I sodium‐phosphate cotransporter (NPT1), a protein initially characterized as phosphate transporter, is expressed at the apical membrane of renal proximal tubular cells and mediated the transport of organic anions (Uchino et al. Biochem Biophys Res Commun, 2000). The predicted amino acid sequence of NPT1 exhibited 60–65% identity to that of OATv1, a voltage‐driven organic anion transporter identified in pig kidney. NPT1 is suggested to be the human orthologue of OATv1 (Jutabha et al. J Biol Chem, 2003). To clarify the functional properties of NPT1 in comparison to OATv1, we used HEK293 expressing either OATv1 or NPT1 as an expression system. NPT1 showed high affinity transport of estrone sulfate, as shown in that of OATv1. The transport was Na+‐independent and enhanced at high concentrations of extracellular potassium. This finding is the first report supporting the functional property of NPT1 as voltage‐driven organic anion transport.