Glycolipid-independent sorting of a secretory glycoprotein to the apical surface of polarized epithelial cells.

Proteins attached to the membrane by a glycosylphosphatidylinositol (GPI)-anchor cluster together with glycolipids in detergent-insoluble complexes at the site of sorting in the trans-Golgi network. This process has been shown to be critical for the targeting of these proteins to the apical cell surface in polarized epithelial cells. We show in this study that gp80 (clusterin), an apically secreted glycoprotein, is not included in detergent-insoluble complexes in Madin-Darby canine kidney cells. Furthermore in Fisher rat thyroid cells, which target GPI-anchored proteins preferentially to the basolateral cell surface, gp80 is secreted apically. Together these results suggest that this secretory glycoprotein and GPI-linked proteins use different mechanisms to reach the apical membrane.