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Journal of Biochemistry Advance Access first published online on November 16, 2007
This version published online on November 20, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm221
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© 2007 The Japanese Biochemical Society

JB Minireview

Expression and function of the HNK-1 carbohydrate

Ippei Morita1, Yasuhiko Kizuka1, Shinako Kakuda2 and Shogo Oka2

1Department of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, and 2 Department of Biological Chemistry, Human Health Science, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan.

Address for correspondence and proofs: Shogo Oka, Ph.D., Department of Biological Chemistry, Human Health Science, Graduate School of Medicine, Kyoto University, Kyoto 606-8507, Japan. Tel & Fax: +81-75-751-3959, E-mail: shogo{at}hs.med.kyoto-u.ac.jp

Received October 25, 2007; Accepted November 8, 2007


  Abstract

Glycosylation is a major post-translational protein modification, especially for cell surface proteins, which play important roles in a variety of cellular functions, including recognition and adhesion. Among them, we have been interested in HNK-1 (Human Natural Killer-1) carbohydrate, which is characteristically expressed on a series of cell adhesion molecules in the nervous system. The HNK-1 carbohydrate has a unique structural feature, i. e., a sulfated glucuronic acid is attached to the non-reducing terminal of an N-acetyllactosamine residue (HSO3-3GlcAß1-3Galß1-4GlcNAc-). We have cloned and characterized the biosynthetic enzymes (two glucuronyltransferases and a sulfotransferase), and also obtained evidence that the HNK-1 carbohydrate is involved in synaptic plasticity and memory formation. In this review, we describe recent findings regarding the expression mechanism and functional roles of this carbohydrate.

Key Words: enzyme complex, glucuronyltransferase, HNK-1, long-term potentiation, substrate specificity


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[Abstract] [Full Text] [PDF]


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