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<title>Biophysical Characteristics of the Pig Kidney Na/Glucose Cotransporter SGLT2 Reveal a Common Mechanism for SGLT1 and SGLT2</title>
<author>
<firstname>Jonna</firstname>
<surname>Terkildsen</surname>
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<shortaffil>Auckland Bioengineering Institute, University of Auckland</shortaffil>
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This CellML model has been curated, the units are consistent and the model runs in COR and PCEnv. This model recreates the published results.
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<title>Model Structure</title>
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Abstract: The Na-dependent, low affinity glucose transporter SGLT2 cloned from pig kidney is 76% identical (at the amino acid level) to its high affinity homologue SGLT1. Using two-microelectrode voltage clamp, we have characterized the presteady-state and steady-state kinetics of SGLT2 expressed in Xenopus oocytes. The kinetic properties of the steady-state sugar-evoked currents as a function of external Na and a-methyl-D-glucopyranoside (aMG) concentrations were consistent with an ordered, simultaneous transport model in which Na binds first. Na binding was voltage-dependent and saturated with hyperpolarizing voltages. Phlorizin was a potent inhibitor of the sugar-evoked currents (Ki ~10 mM) and blocked an inward Na current in the absence of sugar. SGLT2 exhibited Na-dependent presteadystate currents with time constants 3-7 ms. Charge movements were described by Boltzmann relations with apparent valence ~1 and maximal charge transfer ~11 nC, and were reduced by the addition of sugar or phlorizin. The differences between SGLT1 and SGLT2 were that (i) the apparent affinity constant (K0.5) for aMG (~3 mM) was an order of magnitude higher for SGLT2; (ii) SGLT2 excluded galactose, suggesting discrete sugar binding; (iii) K0.5 for Na was lower in SGLT2; and (iv) the Hill coefficient for Na was 1 for SGLT2 but 2 for SGLT1. Simulations of the six-state kinetic model previously proposed for SGLT1 indicated that many of the kinetic properties observed in SGLT2 are expected by simply reducing the Na/glucose coupling from 2 to 1.
</para>
<para>
The original paper reference is cited below:
</para>
<para>
Biophysical Characteristics of the Pig Kidney Na/Glucose Cotransporter SGLT2 Reveal a Common Mechanism for SGLT1 and SGLT2, M. Mackenzie, D.D.F. Loo, M. Panayotova-Heiermann, and E. M. Wright, 1996,
<emphasis>Journal of Biological Chemistry</emphasis>, 271, 32678-32683. <ulink url="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&dopt=AbstractPlus&list_uids=8955098&query_hl=1&itool=pubmed_docsum">PubMed ID: 8955098</ulink>
</para>
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<caption>Schematic diagram of the Mackenzie et al 1996 SGLT2 model. C' represents the external-facing carrier. C'' represents the internal-facing carrier.</caption>
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The Mackenzie et al 1996 quantitative model of the Na/glucose cotransporter (SGLT2).
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This is the CellML description of the Mackenzie et al 1996 quantitative model of the Na/glucose cotransporter (SGLT2).
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<dc:title>
Biophysical Characteristics of the Pig Kidney Na/Glucose Cotransporter SGLT2 Reveal a Common Mechanism for SGLT1 and SGLT2
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<dc:title>Journal of Biological Chemistry</dc:title>
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<bqs:first_page>32678</bqs:first_page>
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