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Research Article |
1 INSERM U426 and Department Physiology, Faculté
de Médecine Xavier Bichat, IFR 02,
Université Paris 7, Paris, France
2 INSERM U380, Institut Cochin de
Génétique
Moléculaire, Paris, France
3 URA 1960 CNRS, Institut Pasteur, Paris, France
4 INSERM U538, Faculté de
Médecine Saint-Antoine, Paris, France
* Author for correspondence (e-mail: terzi{at}cochin.inserm.fr )
Accepted 4 November 2001
It has been reported that vimentin, a cytoskeleton filament that is expressed only in mesenchymal cells after birth, is re-expressed in epithelial cells in vivo under pathological conditions and in vitro in primary culture. Whether vimentin re-expression is only a marker of cellular dedifferentiation or is instrumental in the maintenance of cell structure and/or function is a matter of debate. To address this issue, we used renal proximal tubular cells in primary culture from vimentin-null mice (Vim-/-) and from wild-type littermates (Vim+/+). The absence of vimentin did not affect cell morphology, proliferation and activity of hydrolases, but dramatically decreased Na-glucose cotransport activity. This phenotype was associated with a specific reduction of SGLT1 protein in the detergent-resistant membrane microdomains (DRM). In Vim+/+ cells, disruption of these microdomains by methyl-ß-cyclodextrin decreased SGLT1 protein abundance in DRM, a change that was paralleled by a decrease of Na-glucose transport activity. Importantly, we showed that vimentin is located to DRM, but it disappeared after methyl-ß-cyclodextrin treatment. In Vim-/- cells, supplementation of cholesterol with cholesterol-methyl-ß-cyclodextrin complexes completely restored Na-glucose transport activity. Interestingly, neither cholesterol content nor cholesterol metabolism changed in Vim-/- cells. Our results are consistent with the view that re-expression of vimentin in epithelial cells could be instrumental to maintain the physical state of rafts and, thus, the function of DRM-associated proteins.
Key words: Vimentin, Rafts, SGLT1
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