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Reduced Amelogenin-MMP20 Interactions in Amelogenesis Imperfecta

¹ Department of Orofacial Sciences and
² Department of Cell and Tissue Biology, School of Dentistry, University of California at San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143, USA; and
³ Department of Biochemistry and Biophysics, School of Medicine, University of California at San Francisco, CA, USA

^* corresponding author, Wu.Li{at}ucsf.edu

Amelogenin with a proline 41 to threonine mutation (P41T) is hydrolyzed at a lower rate by matrix metalloproteinase 20 (MMP20), resulting in an inherited tooth enamel defect, amelogenesis imperfecta (AI). The aim of this study was to elucidate the effect of P41T on the interactions between amelogenin and MMP20, which may contribute to the formation of this type of AI. The interactions of a recombinant wild-type human amelogenin and its P41T mutant with recombinant human MMP20 were compared by substrate competition assay, pull-down assay, and surface plasmon resonance (SPR). The results showed that the binding of the P41T mutant amelogenin for MMP20 was significantly lower than that of wild-type amelogenin. Our study supports a model in which the P41T mutation reduces the interactions between amelogenin and MMP20, leading to decreased degradation of amelogenin by MMP20, and resulting in AI.

KEY WORDS: amelogenin • matrix metalloproteinase 20 • protein interaction • tooth enamel • biomineralization • amelogenesis imperfecta