PMID: 9649580Jul 3, 1998Paper

The voltage dependence of a cloned mammalian renal type II Na+/Pi cotransporter (NaPi-2)

The Journal of General Physiology
Ian C ForsterH Murer

Abstract

The voltage dependence of the rat renal type II Na+/Pi cotransporter (NaPi-2) was investigated by expressing NaPi-2 in Xenopus laevis oocytes and applying the two-electrode voltage clamp. In the steady state, superfusion with inorganic phosphate (Pi) induced inward currents (Ip) in the presence of 96 mM Na+ over the potential range -140 </= V </= +40 mV. With Pi as the variable substrate, the apparent affinity constant (KmPi) was strongly dependent on Na+, increasing sixfold for a twofold reduction in external Na+. KmPi increased with depolarizing voltage and was more sensitive to voltage at reduced Na+. The Hill coefficient was close to unity and the predicted maximum Ip (Ipmax) was 40% smaller at 50 mM Na+. With Na+ as the variable substrate, KmNa was weakly dependent on both Pi and voltage, the Hill coefficient was close to 3 and Ipmax was independent of Pi at -50 mV. The competitive inhibitor phosphonoformic acid suppressed the steady state holding current in a Na+-dependent manner, indicating the existence of uncoupled Na+ slippage. Voltage steps induced pre-steady state relaxations typical for Na+-coupled cotransporters. NaPi-2-dependent relaxations were quantitated by a single, voltage-dependent exponential. At 96 mM Na+...Continue Reading

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Citations

Mar 8, 2007·The Journal of Membrane Biology·Ian C ForsterJürg Biber
Apr 20, 2007·The Journal of Membrane Biology·Andrea BacconiIan C Forster
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May 10, 2003·Pflügers Archiv : European journal of physiology·Katja KöhlerHeini Murer

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