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AJP - Regulatory, Integrative and Comparative Physiology, Vol 273, Issue 1 134-R142, Copyright © 1997 by American Physiological Society
ARTICLES |
H. Kipp, E. Kinne-Saffran, C. Bevan and R. K. Kinne
Max-Planck-Institut fur Molekulare Physiologie, Abteilung Epithelphysiologie, Dortmund, Germany.
We have investigated the properties of the skate (Raja erinacea) and shark (Squalus acanthias) kidney Na(+)-D-glucose cotransporters (SGLT) in uptake studies of radiolabeled substrates into isolated renal brush-border membrane vesicles (BBMV). Scatchard plot analysis of the substrate dependence revealed that the Na(+)-D-glucose cotransporter population is homogenous within each species. Skate BBMV showed a relatively high affinity for D-glucose [Michaelis constant (K(m)) = 0.12 mM] with an apparent coupling ratio of approximately 2 Na+ to 1 D-glucose, whereas the shark transporter was much lower in affinity (K(m) = 1.90 mM) and had a lower coupling ratio, more like 1 Na+ to 1 D-glucose. These characteristics resemble the properties of SGLT1 and SGLT2, which are known to coexist in the mammalian kidney. Inhibitor studies using sugar analogs and glucosides suggested structural differences of the D-glucose binding site among these transporters, whereas the hydrophobic transporter domains in the vicinity of the D-glucose binding site appeared to be similar. In the high-affinity skate system, D-glucose was recognized by hydrogen bonds to the hydroxy groups at C-2, C-3, and C-4 and by hydrophobic interaction with the C-6 methylene group. In contrast, the low-affinity shark system seemed to lack the hydrophobic recognition motif for the C-6 methylene group of D-glucose.
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H. Kipp, S. Khoursandi, D. Scharlau, and R. K. H. Kinne More than apical: distribution of SGLT1 in Caco-2 cells Am J Physiol Cell Physiol, October 1, 2003; 285(4): C737 - C749. [Abstract] [Full Text] [PDF] |
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