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- W1999970946 abstract "The myo-inositol molecule (MI) is isomerous to glucose and serves as a compatible osmolyte involved in cell volume regulation and as a precursor of important signalling molecules (inositol phosphates, phosphatidylinositols etc.). hSMIT2 (the product of SLC5A11) is a secondary active MI transporter expressed in the apical membranes of small intestine and proximal tubule, and the two-electrode voltage-clamp technique was used to characterize hSMIT2’s electrogenic properties after expression in Xenopus oocytes. As previously observed for the Na/glucose cotransporter (SGLT1, 49% identical with hSMIT2), hSMIT2 has a 2 Na+: 1 sugar stoichiometry, is inhibited by phlorizin and, in the absence of substrate, exhibits large phlorizin-sensitive pre-steady-state currents with fast (∼2 ms), medium (∼10 ms) and slow components (∼150 ms). The fact that the charge movement recorded during a negative voltage pulse (Qon) can be up to 4 times larger than the charge movement upon return to the normal holding potential (Qoff) indicates that at least a component of the transient current does not represent displacement of a charge associated with the transporter across a fraction of the membrane electrical field. If the slow component of the transient current is omitted from the analysis, Qon equals Qoff and a 5 state kinetic model can accurately reproduce the electrogenic properties of hSMIT2. The overall resulting model indicates that SMIT2 experiences a slow conformational change of the empty transporter with a voltage-dependent intermediate state followed by a fast Na binding reaction and a slower MI binding step. The slow component of the transient currents is thought to represent a slow relaxation of the hSMIT2 leak current which is relatively large (i.e. 4 times the amplitude of typical SGLT1 leak currents)." @default.
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- W1999970946 date "2009-02-01" @default.
- W1999970946 modified "2023-10-18" @default.
- W1999970946 title "The Transport Mechanism of the Human Sodium Myo-Inositol Cotransporter 2 (hSMIT2)" @default.
- W1999970946 doi "https://doi.org/10.1016/j.bpj.2008.12.3618" @default.
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