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Glycobiology Advance Access published online on February 8, 2008
Glycobiology, doi:10.1093/glycob/cwn012
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Laminin-1 is a novel carrier glycoprotein for the non-sulfated HNK-1 epitope in mouse kidney

Yasuhiko Kizuka1, Kyoko Kobayashi1, Shinako Kakuda2, Yukari Nakajima3, Satsuki Itoh3, Nana Kawasaki3 and Shogo Oka2

1 Department of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501
2 Department of Biological Chemistry, Human Health Science, Graduate School of Medicine, Kyoto University, Kyoto 606-8503, Japan
3 Division of Biological Chemistry and Biologicals, National Institute of Health Sciences, Tokyo 158-8501, Japan

Address for correspondence and proofs: Shogo Oka, Ph.D., Department of Biological Chemistry, Human Health Science, Graduate School of Medicine, Kyoto University, Kyoto 606-8503, Japan. Tel&Fax: +81-75-751-3959; E-mail: shogo{at}hs.med.kyoto-u.ac.jp

Received on October 5, 2007; accepted on February 2, 2008

The HNK-1 epitope has a unique structure comprising sulfated trisaccharide (HSO3–3GlcAβ1–3Galβ1–4GlcNAc) and two glucuronyltransferases (GlcAT-P and GlcAT-S) are key enzymes for its biosynthesis. However, the different functional roles of these enzymes in the biosynthesis remain unclear. Recently, we reported that a non-sulfated form of this epitope, which is biosynthesized by GlcAT-S but not by GlcAT-P, is expressed on two metallo-proteases in mouse kidney. In this study, we found that a novel glycoprotein carrying the non-sulfated HNK-1 epitope in mouse kidney was enriched in the nuclear fraction. The protein was affinity-purified and identified as laminin-1, and we also confirmed the N-linked oligosaccharide structure including non-sulfated HNK-1 epitope derived from laminin-1 by mass spectrometry. Curiously, immunofluorescence staining of kidney sections revealed that laminin-1 appeared not to be co-localized with the non-sulfated HNK-1 epitope. However, proteinase treatment strengthened the signals of both laminin-1 and the non-sulfated HNK-1 epitope, resulting in overlapping of them. These results indicate that the non-sulfated HNK-1 epitope on laminin-1 is usually embedded and masked in the robust basement membrane in tight association with other proteins. To clarify the associated proteins and the functional role of the carbohydrate epitope, we investigated the interaction between laminin-1 and alpha-dystroglycan through their glycans in mouse kidney using the overlay assay technique. We obtained evidence that glucuronic acid as well as sialic acid inhibited this interaction, suggesting that the non-sulfated HNK-1 epitope on laminin-1 may regulate its binding and play a role in maintenance of the proper structure in the kidney basal lamina.

Key words: dystroglycan / glucuronyltransferase / HNK-1 / laminin


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