SLC35B2 Inhibitors

Chemical inhibitors of SLC35B2 can exert their inhibitory action through various mechanisms, each targeting different aspects of the glycosylation process in which SLC35B2 is a key player. Tunicamycin, for example, inhibits SLC35B2 by impeding the formation of dolichol-linked oligosaccharides, which are precursors necessary for N-linked glycosylation, a pathway directly involving SLC35B2. Swainsonine and castanospermine exert their effects by inhibiting the processing of N-linked glycans, which SLC35B2 helps transport within the cell. This disruption hinders the maturation of glycoproteins that rely on SLC35B2's proper functioning. Similarly, deoxynojirimycin and deoxymannojirimycin inhibit glycosidase enzymes, crucial for the glycan processing that SLC35B2 regulates, thus impairing the protein's ability to modulate glycan transport.

Kifunensine targets SLC35B2 by inhibiting the mannosidase in the endoplasmic reticulum, a critical enzyme for glycan processing involving SLC35B2, while brefeldin A disrupts the Golgi apparatus structure, where SLC35B2 is localized and active. This leads to a malfunction in glycan transport, a key process mediated by SLC35B2. Nojirimycin works by inhibiting glycosidase activity, which is important for the assembly and modification of glycans, processes in which SLC35B2 is involved. Celgosivir, similar to deoxynojirimycin, impedes glucosidase enzymes, thereby influencing the glycan folding and assembly pathways where SLC35B2 operates. NB-DNJ, another glycosidase inhibitor, hinders glycan processing and transport, which SLC35B2 helps regulate. Lastly, salicylaldehyde forms Schiff bases with sugar aldehydes, a reaction that impacts glycan synthesis and transport, thus inhibiting the functional capacity of SLC35B2 in these pathways.