Endoplasmic reticulum-to-cytosol transport of free polymannose oligosaccharides in permeabilized HepG2 cells.

AUTOR(ES)

Moore, S E

RESUMO

Free polymannose oligosaccharides have recently been localized to both the vesicular and cytosolic compartments of HepG2 cells. Here we investigated the possibility that free oligosaccharides originating in the lumen of the endoplasmic reticulum (ER) are transported directly into the cystosol. Incubation of permeabilized cells in the absence of ATP at 37 degrees C led to the intravesicular accumulation of free Man9GlcNAc2 which was generated from dolichol-linked oligosaccharide in the ER. This oligosaccharide remained stable within the permeabilized cells unless ATP was added to the incubations at which time the Man9GlcNac2 was partially converted to Man8GlcNAc2, and both these components were released from an intravesicular compartment into the cytosolic compartment of permeabilized cells. In contrast, when permeabilized cells, primed with either free triglucosyl-oligosaccharide or a glycotripeptide, were incubated with ATP both these structures remained associated with the intravesicular compartment. As the conditions in which free oligosaccharides were transported out of the intravesicular compartment into the cytosolic compartment did not permit vesicular transport of glycoproteins from the ER to the Golgi apparatus our data demonstrate the presence of a transport process for the delivery of free polymannose oligosaccharides from the ER to the cytosol.

Documentos Relacionados

• Isolation of the tissue factor inhibitor produced by HepG2 hepatoma cells.
• Transfer of retinol-binding protein from HepG2 human hepatoma cells to cocultured rat stellate cells.
• Immunoelectron microscopic localization of the ubiquitin-activating enzyme E1 in HepG2 cells.
• Mitogenic effects of coagulation factor XII and factor XIIa on HepG2 cells.
• alpha-Fucose-mediated binding and degradation of tissue-type plasminogen activator by HepG2 cells.