title: Proteoglycan synthesis and Golgi organization in polarized epithelial cells.
abstract: A large number of complex glycosylation mechanisms take place in the Golgi apparatus. In epithelial cells, glycosylated protein molecules are transported to both the apical and the basolateral surface domains. Although the prevailing view is that the Golgi apparatus provides the same lumenal environment for glycosylation of apical and basolateral cargo proteins, there are indications that proteoglycans destined for the two opposite epithelial surfaces are exposed to different conditions in transit through the Golgi apparatus. We will here review data relating proteoglycan and glycoprotein synthesis to characteristics of the apical and basolateral secretory pathways in epithelial cells.
authors.affiliation: Department of Molecular Biosciences, University of Oslo, Norway. gunnar.dick@imbv.uio.no
authors.forename: Gunnar
authors.initials: G
authors.lastname: Dick
authors.forename: Linn K
authors.initials: LK
authors.lastname: Akslen-Hoel
authors.forename: Frøy
authors.initials: F
authors.lastname: Grøndahl
authors.forename: Ingrid
authors.initials: I
authors.lastname: Kjos
authors.forename: Kristian
authors.initials: K
authors.lastname: Prydz
mesh_terms: D000818:Animals; D001692:Biological Transport; D016764:Cell Polarity; D011508:Chondroitin Sulfate Proteoglycans / Q000378:metabolism; D004285:Dogs; D004847:Epithelial Cells / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism*; D019812:Heparan Sulfate Proteoglycans / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D061985:Madin Darby Canine Kidney Cells; D011509:Proteoglycans / Q000096:biosynthesis* / Q000378:metabolism
chemical_list: D011508:Chondroitin Sulfate Proteoglycans; D006025:Glycosaminoglycans; D019812:Heparan Sulfate Proteoglycans; D011509:Proteoglycans