Reduced amelogenin-MMP20 interactions in amelogenesis imperfecta

被引：13

作者：

Tanimoto, K. ^{[1
]}

Le, T. ^{[1
]}

Zhu, L. ^{[1
]}

Witkowska, H. E. ^{[2
]}

Robinson, S. ^{[2
]}

Hall, S. ^{[2
]}

Hwang, P. ^{[3
]}

DenBesten, P. ^{[1
]}

Li, W. ^{[1
]}

机构：

[1] Univ Calif San Francisco, Dept Orofacial Sci, San Francisco, CA 94143 USA

[2] Univ Calif San Francisco, Dept Cell & Tissue Biol, Sch Dent, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Dept Biochem & Biophys, Sch Med, San Francisco, CA 94143 USA

来源：

JOURNAL OF DENTAL RESEARCH | 2008年 / 87卷 / 05期

关键词：

amelogenin; matrix metallo proteinase 20; protein interaction; tooth enamel; biomineralization; amelogenesis imperfecta;

D O I：

10.1177/154405910808700516

中图分类号：

R78 [口腔科学];

学科分类号：

1003 ;

摘要：

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 wildtype 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.

引用

页码：451 / 455

页数：5

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