Wang Hong-Jun, Tannukit Sissada, Wen Xin, Shapiro Jason L, Snead Malcolm L, Paine Michael L
Center for Craniofacial Molecular Biology, University of Southern California, School of Dentistry, Los Angeles, CA 90033, USA.
Eur J Oral Sci. 2006 May;114 Suppl 1:276-9; discussion 285-6, 382. doi: 10.1111/j.1600-0722.2006.00289.x.
The established structural proteins of the enamel matrix are amelogenin, ameloblastin, and enamelin. Historically, tuftelin and tuftelin-interacting protein 11 (TFIP11) have also been discussed as possible enamel proteins. Protein complexes are achieved by protein-protein interactions, and it is protein complexes that control biomineralization. The purpose of our recent studies was to catalog protein partners for these proteins that are, or have been, implicated in tooth formation. We used the sensitive yeast two-hybrid assay to identify proteins that interact directly with amelogenin, ameloblastin, enamelin, the leucine-rich amelogenin peptide (LRAP) and TFIP11. In this manuscript we refer to, or document, potential protein partners for the proteins listed above. The yeast two-hybrid assay may ultimately prove to be a valuable proteomics methodology for using to decipher molecular events that ultimately result in enamel biomineralization.
釉质基质中已确定的结构蛋白是釉原蛋白、成釉蛋白和釉蛋白。从历史上看,牙丛蛋白和牙丛蛋白相互作用蛋白11(TFIP11)也曾被作为可能的釉质蛋白进行讨论。蛋白质复合物是通过蛋白质-蛋白质相互作用形成的,而正是蛋白质复合物控制着生物矿化。我们近期研究的目的是梳理出这些已参与或曾参与牙齿形成的蛋白质的蛋白质相互作用伙伴。我们使用灵敏的酵母双杂交试验来鉴定与釉原蛋白、成釉蛋白、釉蛋白、富含亮氨酸的釉原蛋白肽(LRAP)和TFIP11直接相互作用的蛋白质。在本手稿中,我们提及或记录了上述蛋白质的潜在蛋白质相互作用伙伴。酵母双杂交试验最终可能会被证明是一种用于解读最终导致釉质生物矿化的分子事件的有价值的蛋白质组学方法。