Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial cell line.

• DOI: 10.1073/pnas.85.24.9557
• Publication Date: 2006-05-31T10:47:28Z
• Authors: M P Lisanti; M Sargiacomo; L Graeve; A R Saltiel; E Rodriguez-Boulan
• Keywords: Apical cell; Cell membrane; Cell polarity; Apical membrane; Epithelial polarity

Polarized epithelial cell monolayers contain two distinct plasma membrane domains as delineated by the presence of tight junctions--i.e., an apical surface that faces external environment and a basolateral functions both in cell-cell contact cell-substrate attachment. Central to understanding polarity is question how such cell-surface specializations are generated. A different class glycoproteins has recently emerged may yield new insight into mechanism underlying biogenesis this polarity. Members large extracellular protein domain linked via glycosyl-phosphatidylinositol. Using polarized renal line (Madin-Darby canine kidney), we identified endogenous glycosyl-phosphatidylinositol-anchored proteins through release phosphatidylinositol-specific phospholipase C. Six 110, 85, 70, 55, 38, 35 kDa were appeared be restricted surface. Our data consistent with notion glycosyl-phosphatidylinositol anchor necessary information for "targeting"