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J. Biol. Chem., Vol. 275, Issue 25, 18785-18793, June 23, 2000
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-O-benzyl Inhibits Sialylation of
de Novo Synthesized Apical but Not Basolateral
Sialoglycoproteins and Blocks Lysosomal Enzyme Processing in a
Post-trans-Golgi Network Compartment*
,
From the Unitat de Biologia Cel.lular i Molecular, Institut
Municipal d'Investigació Mèdica, Universitat Pompeu Fabra,
carrer Dr. Aiguader, 80, 08003 Barcelona, Spain
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-
-O-benzyl reversibly inhibits sialylation and
causes the accumulation of apical glycoproteins in cytoplasmic vesicles. We have analyzed at the biochemical level the effects of
GalNAc--O-benzyl on glycoprotein processing. Both apical
and basolateral membrane glycoproteins were sialylated, but
GalNAc--O-benzyl selectively inhibited the sialylation
of apical glycoproteins. In addition, lysosomal -glucosidase, which
is partially targeted to the apical membrane, was abnormally
processed leading to the accumulation of an immature molecular
species. Several findings support the conclusion that accumulation of
this protein occurs in a post-trans-Golgi network (TGN) compartment: 1)
it is partially sialylated; 2) it does not occur when glycoprotein exit
from the TGN is blocked at 20 °C; 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--O-benzyl treatment. In conclusion,
GalNAc--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.
Recipient of a predoctoral fellowship from the MUTIS Program.
§
To whom correspondence should be addressed. Tel.: 34-93-2211009;
Fax: 34-93-2213237; E-mail: preal@imim.es.
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