Proteoglycan Synthesis and Golgi Organization in Polarized Epithelial Cells

Overview

Journal J Histochem Cytochem

Publisher Sage Publications

Specialty Biochemistry

Date 2012 Sep 4

PMID 22941419

Citations 17

Authors

Gunnar Dick

Linn K Akslen-Hoel

Froy Grondahl

Ingrid Kjos

Kristian Prydz

Affiliations

Soon will be listed here.

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.

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