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A more recent version of this article appeared on January 1, 2004
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Submitted on April 8, 2003
Revised on September 19, 2003
Accepted on September 19, 2003
1 UMR INSERM U505, Université Pierre et Marie Curie, Laboratoire de Pharmacologie Cellulaire et Moléculaire de l’EPHE, 15 rue de l’Ecole de Médecine, 75006 Paris, France; Etienne Morel is recipient of a MNRT fellowship
2 UMR INSERM U505, Université Pierre et Marie Curie, Laboratoire de Pharmacologie Cellulaire et Moléculaire de l’EPHE, 15 rue de l’Ecole de Médecine, 75006 Paris, France
* Corresponding author. E-mail address: fransisco.delers-u505{at}bhdc.jussieu.fr.
Enterocytes are highly polarized cells that transfer nutrients across the intestinal epithelium from the apical to the baso-lateral pole. Apolipoprotein B (apoB) is a secretory protein that plays a key role in the trans-epithelial transport of dietary fatty acids as triacylglycerol. The evaluation of the control of apoB traffic by lipids is therefore of particular interest. To get a dynamic insight into this process, we used the enterocytic Caco-2 cells cultured on microporous filters, a system in which the apical and basal compartments can be delimited. Combining biochemical and morphological approaches, our results showed that, besides their role in protection from degradation, lipids control the intracellular traffic of apoB in enterocytes. A supply of fatty acids and cholesterol is sufficient for the export of apoB from the ER and its postGolgi traffic up to the apical brush-border domain, where it remains until an apical supply of complex lipid micelles signals its chase down to the basolateral secretory domain. This downward traffic of apoB involves a microtubule-dependent process. Our results demonstrate an enterocyte-specific bidirectional process for the lipid-dependent traffic of a secretory protein.
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