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. 2014 Dec 15;111(52):E5697–E5705. doi: 10.1073/pnas.1416675112

Table 2.

Glycosylation inhibitors

Inhibitor and effective sites Expected structure Percent decrease in 5-HT uptake rates of trophoblasts
PNGase F cleaves between the innermost GlcNAc and asparagine residues from N-linked glycoproteins Nascent SERT (no glycosylation)
Endoglycosidase H cleaves the bond between two GlcNAc subunits, N-acetylglucosamine residue remaining on the asparagine (46). GlcNAc- SERT
Tunicamycin, a competitive inhibition of UDP-GlcNAc, prevents the glycosyl modification at initial step (46). Nascent SERT (no glycosylation) 35–72.3%
Significant (P value <0.001)
Castanospermine, α-glucosidase inhibitor, prevents removal of the glucose residues (46). Glc3Man9GlcNAc2-SERT 28.7%
Not significant (P value = 0.02)
Swainsonine inhibitor of Golgi mannosidase II (46). Man5GlcNAc2-SERT 7.8%
Not significant (P value = 1.54)