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Journal of Dental Research
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Biological

Splicing Determines the Glycosylation State of Ameloblastin

K. Kobayashi1,3, Y. Yamakoshi1, J.C.-C. Hu2, K. Gomi3, T. Arai3, M. Fukae4, P.H. Krebsbach1 and J.P. Simmer1,*

1 Department of Biologic and Materials Sciences, Dental Research Lab, 1210 Eisenhower Place, Ann Arbor, MI 48108, and
2 Department of Orthodontics and Pediatric Dentistry, University of Michigan School of Dentistry, 1011 N. University, Ann Arbor, MI 48109-1078, USA; and
3 Department of Periodontics and Endodontics and
4 Department of Biochemistry, School of Dental Medicine, Tsurumi University, 2-1-3 Tsurumi, Tsurumi-ku, Yokohama 230-8501, Japan

Correspondence: * corresponding author, jsimmer{at}umich.edu

In developing porcine enamel, the space between enamel rods selectively binds lectins and ameloblastin (Ambn) N-terminal antibodies. We tested the hypothesis that ameloblastin N-terminal cleavage products are glycosylated. Assorted Ambn cleavage products showed positive lectin staining by peanut agglutinin (PNA), Maclura pomifera agglutinin (MPA), and Limulus polyphemus agglutinin (LPA), suggesting the presence of an O-linked glycosylation containing galactose (Gal), N-acetylgalactosamine (GalNAc), and sialic acid. Edman sequencing of the lectin-positive bands gave the Ambn N-terminal sequence: VPAFPRQPGTXGVASLXLE. The blank cycles for Pro11 and Ser17 confirmed that these residues are hydroxylated and phosphorylated, respectively. The O-glycosylation site was determined by Edman sequencing of pronase-digested Ambn, which gave HPPPLPXQPS, indicating that Ser86 is the site of the O-linked glycosylation. This modification is within the 15-amino-acid segment (73-YEYSLPVHPPPLPSQ-87) deleted by splicing in the mRNA encoding the 380-amino-acid Ambn isoform. We conclude that only the N-terminal Ambn products derived from the 395-Ambn isoform are glycosylated.

Key Words: ameloblastin • Ambn • sheathlin • enamel • tooth • porcine

Journal of Dental Research, Vol. 86, No. 10, 962-967 (2007)
DOI: 10.1177/154405910708601009
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