Article Abstract:
Membrane transport of epithelial Madin-Darby canine kidney (MDCK) cells was inhibited by anti-N-ethylmaleimide-sensitive factor (NSF) in a permeabilized cell system, but was stimulated by alpha-soluble NSF attachment proteins. However, transport of cells from the trans-Golgi network to the apical cell surface was not affected by these proteins. Apical transport was also not affected by Rab-GDI and tetanus and botulinum neurotoxins which inhibit basolateral transport, suggesting that the Rab-NSF-SNAP-SNARE machinery only operates in basolateral transport.
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Article Abstract:
The addition of N-glycan to proteins helps in protein folding and stabilizing of the protein structure after which the proteins can be transported out of the endoplasmic reticulum. N-glycan is also involved in the transfer of a GlcNAc phosphate to a mannose on the lysosome enzymes. However the proteins that do not undergo glycosylation or use a transport mechanism other than glycosylation have to use a sorting signal other than N-glycan. The transport of apical membrane proteins from the Golgi to the cell surface also involves N-glycan.
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Article Abstract:
All epithelial cells are characterized by specialized junctions, internal architecture and surface polarity which allow them to behave differently at their apical and basal sides. Epithelial cells have a polar cytoplasmic organization and a polar exterior and polarization is regulated by different mechanisms. The mechanism of polarization in four different epithelia is discussed.
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