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Human Amelogenin Degradation by MMP-20 in Tooth Enamel Development Studied by SDS PAGE, MALDI TOF MS and LC MS/MS.

机译:通过SDS页面,MALDI TOF MS和LC MS / MS进行MMP-20在牙釉质开发中通过MMP-20降解人氨基蛋白。

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Tooth enamel is the hardest tissue in the human body: it is built from closely packed, thin elongated hydroxyapatite (HAP) crystals. Biomineralization occurs within an extracellular protein matrix in developing tooth enamel. Initially, amelogenins (Amg) make up more than 90% of total protein in the matrix but in the process of enamel maturation, proteins are removed by proteolysis, mainly mediated by metalloproteinase 20 (MMP-20). Degradation of amelogenin can be altered by mineral binding affecting specificity and rate of proteolysis. Likewise, certain amelogenin mutations are associated with incomplete protein removal resulting in amelogenesis imperfecta. We have investigated the process of proteolysis, by MMP-20, of amelogenin bound to apatite and free in solution and studied the effects of a gene mutation on its degradation.
机译:牙釉质是人体中最难的组织:它是由紧密包装的薄细长羟基磷灰石(HAP)晶体构建的。生物蛋白发生在显影牙釉质中的细胞外蛋白质基质中。最初,Amelogens(AMG)在基质中占总蛋白质的90%以上,但在牙釉质成熟过程中,通过蛋白水解除去蛋白质,主要由金属蛋白酶20(MMP-20)介导。可通过影响特异性和蛋白水解率的矿物结合而改变Amelogenin的降解。同样地,某些氨基蛋白突变与不完全的蛋白质去除相关,导致Amelogesis渗透。我们研究了MMP-20的蛋白质溶解的蛋白质溶液的方法,其结合到磷灰石并在溶液中自由,并研究了基因突变对其降解的影响。

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