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Carbohydrate sulfotransferases in humans: Repertoire and regulation of glycan-lectin interactions
Kim Wai Parn1, Takashi Angata1
1Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan; Chemical Biology and Molecular Biophysics Program, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan.
Background:
Sulfate in glycans often serves as a determinant of glycan-protein interactions underlying mammalian physiology. Sulfated glycoconjugates in mammals encompass proteoglycans, glycoproteins, and glycolipids, and more than 30 sulfotransferases catalyze carbohydrate sulfation.
Scope Of Review:
We summarize the repertoire of carbohydrate sulfotransferases in humans and their relevance to human physiology, focusing on those that modify N- and O-glycans on glycoproteins and modulate glycan-protein interactions.
Major Conclusions:
Sulfate is indispensable in some glycan-protein interactions, whereas sialic acid can replace it in some others. The presence of both sulfate and sialic acid enhances some interactions. Regulation of glycan-protein interactions by the combination of sulfate and sialic acid has been actively investigated, while in vivo proof of such interactions may still be limited, particularly for those discovered recently.
General Significance:
A deeper understanding of glycan-protein interactions regulated by sulfation will advance our understanding of human physiology and contribute to improving human health.
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