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Papers In Press, published online ahead of print April 5, 2000
Unitat de Biologia Cel.lular i Molecular, Institut Municipal d'Investigacio Medica, Barcelona, Barcelona 08003
Corresponding Author: preal{at}imim.es
Glycosylation plays an important role in glycoprotein traffic. Our previous work has shown that long-term treatment of mucus-secreting HT-29 cells with GalNAc-a-O-benzyl reversibly inhibits sialylation and causes the accumulation of apical glycoproteins in cytoplasmic vesicles. We have analysed at the biochemical level the effects of GalNAc-a-O-benzyl on glycoprotein processing. Both apical and basolateral membrane glycoproteins were sialylated but GalNAc-a-O-benzyl selectively inhibited the sialylation of apical glycoproteins. In addition, lysosomal a-glucosidase - which is partially targeted to the apical membrane - was abnormally processed leading to the accumulation of an immature molecular species. Several findings support that accumulation of this protein occurs in a post-TGN compartment: 1) it is partially sialylated; 2) it does not occur when glycoprotein exit from the TGN is blocked at 20ºC; 3) upon Triton X-114 partition, it distributes to the aqueous phase, a characteristic that is acquired in a post-TGN compartment; and 4) its appearance is inhibited when cells are cultured in the presence of NH4Cl. The processing of cathepsin D was also found to be affected by GalNAc-a-O-benzyl treatment. In conclusion, GalNAc-a-O-benzyl selectively inhibits sialylation of apical glycoproteins and perturbs lysosomal enzyme processing; these effects occur in a post-TGN acidic compartment and are reminiscent of the alterations found in sialic acid storage diseases.
J. Biol. Chem, 10.1074/jbc.M000510200
Submitted on January 24, 2000
Revised on April 3, 2000
Accepted on April 5, 2000
GalNAc-a-O-Benzyl inhibits sialylation of de novo synthesized apical, but not basolateral, sialoglycoproteins and blocks lysosomal enzyme processing in a post-TGN compartment
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