| Literature DB >> 22941419 |
Gunnar Dick1, Linn K Akslen-Hoel, Frøy Grøndahl, Ingrid Kjos, Kristian Prydz.
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.Mesh:
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Year: 2012 PMID: 22941419 PMCID: PMC3527882 DOI: 10.1369/0022155412461256
Source DB: PubMed Journal: J Histochem Cytochem ISSN: 0022-1554 Impact factor: 2.479