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1 Department of Toxicology, University of Zaragoza, Zaragoza, Zaragoza, Spain
2 Department of Pharmacology, University of Zaragoza, Zaragoza, Zaragoza, Spain
3 Department of Physiology, University of Zaragoza, Zaragoza, Zaragoza, Spain
4 Department of Genetics, University of Zaragoza, Zaragoza, Zaragoza, Spain
5 Department of Anatomy, University of Zaragoza, Zaragoza, Zaragoza, Spain
* To whom correspondence should be addressed. E-mail: sorribas{at}unizar.es.
Renal reabsorption is the main mechanism that controls mannose homeostasis. This takes place through a specific sodium-coupled uphill transport system, the molecular identity of which is unknown. We have prepared and screened a size-selected rat kidney cortex cDNA library through the expression of mannose transport in Xenopus laevis oocytes. We have identified a membrane protein that induces high affinity and specific Na-dependent transport of D-mannose and D-glucose in Xenopus laevis oocytes, most likely through stimulation of the capacity of an endogenous transport system of the oocyte. Sequencing has revealed that the cDNA encodes the counterpart of the human membrane associated protein MAP17, previously known by its overexpression in renal, colon, lung and breast carcinomas. We show that MAP17 is a 12.2 kDa non-glycosylated membrane protein that locates to the brush-border plasma membrane and the Golgi apparatus of transfected cells and that it is expressed in the proximal tubules of the kidney cortex and in the spermatids of the seminiferous tubules. It spans twice the cell membrane with both termini inside the cell and seems to form homodimers through the intracellular Cys-55, a residue also involved in transport expression. MAP17 is responsible for the mannose transport expression in oocytes by rat kidney cortex mRNA. The induced transport has the functional characteristics of an SGLT transporter, because D-glucose and 
-methyl-D-glucopyranoside are also accepted substrates that are inhibited by phloridzin. The corresponding transporter from the proximal tubule remains to be identified, but it is different from the known mammal SGLT-1, -2 and -3.
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