Functional glycomics: Application to medical science and hepatology

Abstract

Glycomics refers to the comprehensive analysis of glycans. Recent progress in glycotechnology enables the determination of a variety of biological functions of glycans. Among different glycosylation patterns, certain types of aberrant glycosylation are linked to cancer and/or inflammation, and thus have biological importance. Glycotechnology has been applied to many fields of medical science, including hepatology. In particular, dramatic changes in glycosylation are observed in the progression of liver diseases. As the liver produces so many serum glycoproteins, changes in glycosylation of these proteins might provide useful disease biomarkers. Furthermore, many patients with genetic diseases of glycosylation who have liver dysfunction have been found as a result from whole genome sequencing, and various kinds of glycotherapy have been developed, especially in immunotherapy. In this review, we describe our basic knowledge of glycobiology and discuss the application of these data to medical science, especially hepatology.

Exploring the carbohydrate‐binding ability of Canavalia bonariensis lectin in inflammation models

“…The mechanism that justifies the edematogenic effect of CaBo may not be clear, however, in vivo tests added to in silico analyses of the carbohydrate‐binding ability of CaBo suggests that the interaction of lectin with complex N ‐glycans contributes to the induction of the process inflammatory. It is also important to note that other studies have already reported that pro‐inflammatory cytokines induce changes in cell‐surface N ‐glycosylation of endothelial cells, suggesting that glycosylation might contribute to inflammatory vascular diseases 33 . These events suggest a double participation of CaBo's CRD in these biological processes.…”

Abnormal fucosylation of alpha‐fetoprotein in patients with nonalcoholic steatohepatitis

“…It is also known to be a marker of a hypercarcinogenic state in patients infected with the hepatitis C virus and who have achieved a sustained virologic response 7–9 . The tumor marker AFP has one N ‐glycan at Asn 232, and core fucosylation of the glycan is observed in some HCC patients 10–12 . Fucosylated AFP is known to be a marker of poor prognosis.…”

Screening siRNAs against host glycosylation pathways to develop novel antiviral agents against hepatitis B virus

“…Glycosylation is one of the most important post‐translational modifications of proteins and lipids. Glycolipids, including sphingolipids, are formed through the addition of short sugar chains and are mostly involved in cell signaling 15 …”

“…Glycolipids, including sphingolipids, are formed through the addition of short sugar chains and are mostly involved in cell signaling. 15 Unique oligosaccharide structures are defined by the sequential reaction of glycosyltransferases and processing glycosidases. 15 In many infectious diseases caused by either viruses or bacteria, pathogen glycoproteins play important roles during the infection cycle, ranging from entry to successful intracellular replication and host immune evasion.…”

“…15 Unique oligosaccharide structures are defined by the sequential reaction of glycosyltransferases and processing glycosidases. 15 In many infectious diseases caused by either viruses or bacteria, pathogen glycoproteins play important roles during the infection cycle, ranging from entry to successful intracellular replication and host immune evasion. 16 HBV relies on N-linked glycosylation for crucial functions such as entry into host cells, proteolytic processing and protein trafficking.…”