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Transglutaminase Crosslinking of SIBLING Proteins in Teeth

¹ Division of Oral Biology, Faculty of Dentistry, McGill University, Strathcona Bldg.-Room M34, 3640 University Street, Montreal, QC, Canada H3A 2B2;
² Division of Experimental Medicine, Department of Medicine, Faculty of Medicine, McGill University, QC, Canada; and
³ Department of Anatomy and Cell Biology, Faculty of Medicine, McGill University, Montreal, QC, Canada;

^* corresponding author, mari.kaartinen{at}mcgill.ca

Transglutaminase 2 (TG2), a protein-crosslinking enzyme, participates in extracellular matrix maturation and cell adhesion in cartilage and bone. We hypothesized that TG2 has similar roles in teeth. A TG activity assay and immunoblotting of rat tooth extracts showed TG activity and the presence of high-molecular-weight forms of the SIBLING (Small Integrin-Binding LIgand N-linked Glycoprotein) proteins: dentin matrix protein 1 (DMP1), dentin phosphoprotein (DPP), and bone sialoprotein (BSP). DMP1 and BSP, each containing both glutamine and lysine residues critical for crosslink formation, readily formed polymers in vitro when incubated with TG2. The ability of glutamine-lacking DPP to form polymers in vitro and in vivo demonstrates that it could act as a lysine donor for crosslinking, potentially having protein crosslinking partner(s) in teeth. Consistent with a role in cell adhesion, the TG2 isoform was co-localized by immunohistochemistry with its substrates at cell-matrix adhesion sites, including along odontoblast tubules (DMP1 and DPP), in the pericellular matrix of cementocytes (DMP1), and in predentin (BSP).

KEY WORDS: transglutaminase • crosslinking • SIBLING proteins • teeth • extracellular matrix

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