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HEPARAN SULFATE GLYCOSAMINOGLYCANS Heparan sulfate (HS) glycosaminoglycans (HSGAGs) are highly complex biopolymers (1, 2). HS structural diversity is characterized by a repeat disaccharide unit of uronic acid (either iduronic or glucuronic acid) linked to a glucosamine (1). Due to the extensive structural diversity of HS resulting from the assembly of 23 distinct disaccharides, it has been called the “most information dense biopolymer in nature” (3, 4), which in turn enables it to interact with a multitude of different proteins. Indeed, the specificity of these interactions would depend on HSGAG composition, tertiary structure, and spacing of binding sites (1). Heparan sulfate glycosaminoglycans play an essential role in key biological processes and are of particular importance to the survival and progress of various cancers (5). Alterations of the HSGAG epitope repertoire were observed both within various normal tissues and between normal and cancerous tissues (6–8). Indeed, some tumors can exhibit unique carbohydrate profile: over-express certain HSGAGs or express unique HSGAG epitopes (9, 10) that can be rarely found in normal tissue (11). In both tumor and normal mammalian tissue, HSGAGs are usually found covalently attached to various core proteins such as heparan sulfate proteoglycans (HSPGs). The two main groups of cell surface expressed HSPGs are the Syndecans (SDCs) and the Glypicans (1). Bearing in mind the alterations of HSGAG epitope repertoire, HSPGs could be considered as self “modifiable” ligands for HSGAG-binding receptors.

frontiers in oncology

Carbohydrate-Mediated Modulation of NK Cell Receptor Function: Structural and Functional Influences of Heparan Sulfate Moieties Expressed on NK Cell Surface