Carbohydrate sulfotransferase 10 (CHST10)

Abstract

The sulfotransferase with the official gene name carbohydrate sulfoctransferase 10 (CHST10) is involved in the biosynthesis of the HNK-1 carbohydrate epitope, originally described as a differentiation antigen specifically expressed on human natural killer (HNK) cells (Abo and Balch 1981). Shortly after, it was discovered that the HNK-1 antibody detected cells and tumors of neuroectodermal origin in addition (Lipinski et al. 1983; Schuller-Petrovic et al. 1983) and that myelin-associated glycoprotein (MAG) was a target (McGarry et al. 1983). From then, research on the HNK-1 epitope focused on the nervous system. The antibody was shown to recognize both glycoproteins and glycolipids, defining HNK-1 as a carbohydrate epitope (Ilyas et al. 1984). An independently isolated antibody called L2 (or 412, L2-412, or HNK-1-412, here further called L2) detected the same carbohydrate epitope as HNK-1 on neural cell adhesion molecule (NCAM), MAG, and L1 (Kruse et al. 1984). Chou et al. (1986) then identified the glycolipid structure that was recognized by the antibody as SO4-3GlcAβ1-3Galβ1-4GlcNAcβ1-3Galβ1-4Glcβ1-Cer. On proteins, the structure has been found on both N-linked (Voshol et al. 1996; Liedtke et al. 2001; Wuhrer et al. 2003) and O-linked glycans. In O-glycans the structure has been identified on O-mannose (Yuen et al. 1997) and mucin-type, O-GalNAc-linked, glycans (Ong et al. 2002). The common structure on glycolipids and glycoproteins is SO4-3GlcAβ1-3Galβ1-4/3GlcNAc (Fig. 92.1). This sulfated trisaccharide is generally defined as the HNK-1 structure. The existence of at least one sulfotransferase transferring sulfate to the C3 position of glucuronic acid, tentatively called the HNK-1 sulfotransferase, could be predicted from this structure.