The HNK-1 epitope was originally described as a marker of a subfraction of human natural killer cells (Abo and Balch 1981). Despite its name, the HNK-1 carbohydrate epitope is found in many tissues but is predominantly expressed in the mammalian nervous system. The expression pattern of the HNK-1 carbohydrate in both the central and peripheral nervous system is spatially and developmentally regulated. In the nervous system the HNK-1 carbohydrate epitope is carried by many neural recognition glycoproteins and is involved in homophilic and heterophilic binding of these proteins (Schachner and Martini 1995). The epitope is characterized by the structure SO4-3GlcAβ1-3Galβ(1-4GlcNAc) at the nonreducing end of glycans found on glycoproteins (N- and O-linked) (Voshol et al. 1996; Wakabayashi et al. 1999) and glycolipids (Chou et al. 1986). The key enzymes in the biosynthesis of HNK-1 carbohydrates are a glucuronyltransferase (GlcA-transferase) (Terayama et al. 1997) (see Chapter 51) and a sulfotransferase, as the underlying lactosamine structure is commonly found in glycoconjugates. The sulfotransferase enzyme catalyzing the transfer of sulfate from the donor substrate 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to the glucuronic acid containing glycolipid or glycoprotein acceptor was first characterized by Chou and Jungalwala (1993), and the cDNA was first cloned by Bakker et al. (1997).


Neural Cell Adhesion Molecule Human Natural Killer Cell Sulfotransferase Activity mRNA AF033827 Heterophilic Binding 
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  1. Abo T, Balch CM (1981) A differentiation antigen of human NK and K cells identified by a monoclonal antibody (HNK-1). J Immunol 127:1024–1029PubMedGoogle Scholar
  2. Bakker H, Friedmann I, Oka S, Kawasaki T, Nifant’ev N, Schachner M, Mantei N (1997) Expression cloning of a cDNA encoding a sulfotransferase involved in the biosynthesis of the HNK-1 carbohydrate epitope. J Biol Chem 272:29942–29946PubMedCrossRefGoogle Scholar
  3. Chou DKH, Jungalwala FB (1993) Characterization and developmental expression of a novel sulfotransferase for the biosynthesis of sulfoglucuronyl glycolipids in the nervous system. J Biol Chem 268:330–336PubMedGoogle Scholar
  4. Chou DKH, Ilyas AA, Evans JE, Costello C, Quarles RH, Jungalwala FB (1986) Structure of sulfated glucuronyl glycolipids in the nervous system reacting with HNK-1 antibody and some IgM paraproteins in neuropathy. J Biol Chem 261:11717–11725PubMedGoogle Scholar
  5. Kruse J, Mailhammer R, Wernecke H, Faissner A, Sommer I, Goridis C, Schachner M (1984) Neural cell adhesion molecules and myelin-associated glycoprotein share a common carbohydrate moiety recognized by monoclonal antibodies L2 and HNK-1. Nature 311:153–155PubMedCrossRefGoogle Scholar
  6. Ong E, Yeh J-C, Ding Y, Hindsgaul O, Fukuda M (1998) Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids. J Biol Chem 273:5190–5195PubMedCrossRefGoogle Scholar
  7. Ong E, Yeh J-C, Ding Y, Hindsgaul O, Pedersen LC, Negishi M, Fukuda M (1999) Structure and function of HNK-1 sulfotransferase: identification of donor and acceptor binding sites by site-directed mutagenesis. J Biol Chem 274:25608–25612PubMedCrossRefGoogle Scholar
  8. Schachner M, Martini R (1995) Glycans and the modulation of neurα1-recognition molecule function. Trends Neurosci 18:183–191PubMedCrossRefGoogle Scholar
  9. Terayama K, Oka S, Seiki T, Miki Y, Nakamura A, Kozutsumi Y, Takio K, Kawasaki T (1997) Cloning and functional expression of novel glucuronyltransferase involved in the biosynthesis of the carbohydrate epitope, HNK-1. Proc Natl Acad Sci USA 94:6093–6098PubMedCrossRefGoogle Scholar
  10. Voshol H, van Zuylen CWEM, Orberger G, Vliegenthart JFG, Schachner M (1996) Structure of the HNK-1 carbohydrate epitope on bovine peripheral myelin glycoprotein P0. J Biol Chem 271:22957–22960PubMedCrossRefGoogle Scholar
  11. Wakabayashi H, Natsuka S, Mega T, Otsuki N, Isaji M, Naotsuka M, Koyama S, Kanamori T, Sakai K, Hase S (1999) Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAβ1-3Galβ1-3(±Siaα2-6)Galβ1-4Xyl. J Biol Chem 274:5436–5442PubMedCrossRefGoogle Scholar
  12. Yamauchi S, Mita S, Matsubara T, Fukuta M, Habuchi H, Kimata K, Habuchi O (2000) Molecular cloning and expression of chondroitin 4-sulfotransferase. J Biol Chem 275:8975–8981PubMedCrossRefGoogle Scholar

Copyright information

© Springer Japan 2002

Authors and Affiliations

  • Hans Bakker
    • 1
    • 2
  1. 1.Plant Research InternationalWageningen University and Research CentreWageningenThe Netherlands
  2. 2.Institut für Physiologische Chemie, Proteinstruktur-OE4315Medizinische Hochschule HannoverHannoverGermany

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