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This Article Full Text Full Text (PDF) All Versions of this Article: 293/6/G1300    most recent 00422.2007v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Aouameur, R. Articles by Lapointe, J.-Y. PubMed PubMed Citation Articles by Aouameur, R. Articles by Lapointe, J.-Y.

MUCOSAL BIOLOGY

SMIT2 mediates all myo-inositol uptake in apical membranes of rat small intestine

¹Groupe d'étude des protéines membranaires (GÉPROM), Département de Physiologie and ²Département de Physique, Université de Montréal, Montréal, Québec, Canada

Submitted 18 September 2007 ; accepted in final form 11 October 2007

This study presents the characterization of myo-inositol (MI) uptake in rat intestine as evaluated by use of purified membrane preparations. Three secondary active MI cotransporters have been identified; two are Na⁺ coupled (SMIT1 and SMIT2) and one is H⁺ coupled (HMIT). Through inhibition studies using selective substrates such as D-chiro-inositol (DCI, specific for SMIT2) and L-fucose (specific for SMIT1), we show that SMIT2 is exclusively responsible for apical MI transport in rat intestine; rabbit intestine appears to lack apical transport of MI. Other sugar transport systems known to be present in apical membranes, such as SGLT1 or GLUT5, lacked any significant contribution to MI uptake. Functional analysis of rat SMIT2 activity, via electrophysiological studies in Xenopus oocytes, demonstrated similarities to the activities of SMIT2 from other species (rabbit and human) displaying high affinities for MI (0.150 ± 0.040 mM), DCI (0.31 ± 0.06 mM), and phlorizin (Pz; 0.016 ± 0.007 mM); low affinity for glucose (36 ± 7 mM); and no affinity for L-fucose. Although these functional characteristics essentially confirmed those found in rat intestinal apical membranes, a unique discrepancy was seen between the two systems studied in that the affinity constant for glucose was 40-fold lower in vesicles (K_i = 0.94 ± 0.35 mM) than in oocytes. Finally, the transport system responsible for the basolateral efflux transporter of glucose in intestine, GLUT2, did not mediate any significant radiolabeled MI uptake in oocytes, indicating that this transport system does not participate in the basolateral exit of MI from small intestine.

brush border; glucose; transport; oocytes; phlorizin