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Journal of Cell Science, Vol 107, Issue 2 553-559, Copyright © 1994 by Company of Biologists

JOURNAL ARTICLES

Sorting of a secretory protein (gp80) to the apical surface of Caco-2 cells

D Appel and C Koch-Brandt
Institut fur Biochemie, J. Gutenberg-Universitat, Mainz, Germany.

We have investigated the synthesis and polarized secretion of the exogenous gp80 glycoprotein complex in the human epithelial adenocarcinoma cell line, Caco-2. gp80 is secreted at the apical surface of Madin-Darby canine kidney (MDCK) cells and should, therefore, display the signal(s) required for sorting into the apical exocytic pathway. In Caco-2 cells, no bona fide secretory protein released preferentially at the apical surface has been described so far. To address the question of whether Caco-2 cells possess a machinery capable of delivery of secretory proteins at the apical surface, we stably transfected the cells with a recombinant gene coding for the gp80 glycoprotein complex. Pulse-chase analysis showed that stably transfected Caco-2 cells secrete gp80 quantitatively into the medium. In polarized layers of filter-grown Caco-2 cells, the protein was secreted predominantly at the apical surface, demonstrating the ability of the cells to efficiently sort secretory proteins directly into the apical exocytic pathway. Our results further demonstrate that the apical targeting information of gp80 recognized by MDCK cells is also recognized by Caco-2 cells.
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This article has been cited by other articles:


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 J. Biol. Chem.Home page
R. Graichen, A. Losch, D. Appel, and C. Koch-Brandt
Glycolipid-independent Sorting of a Secretory Glycoprotein to the Apical Surface of Polarized Epithelial Cells
J. Biol. Chem., July 5, 1996; 271(27): 15854 - 15857.
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© The Company of Biologists Ltd 1994