Study on the Glu-specific protease superfamily mediating dissociation of cell-cell adhesion

谷氨酸特异性丝氨酸肽酶（GluV8）家族的前肽的缩短通常以自催化方式发生。伴随着前肽缩短，前成熟连接变得更容易受到成熟酶的影响。我们证明了在体外Glu特异性内肽酶活性的剥脱毒素（ET）A的第一次，这是大肠杆菌表达的重组ETA和合成肽基底物测定。动物模型显示，蛋白水解活性是皮肤脱落所不可缺少的。此外，我们确定了DPP11和DPP7的特征，并提出了一个新的系统发育的这些家庭分子。

Shortening of the propeptide of Glu-specific serine peptidase(GluV8) family commonly occurred in an auto-catalytic manner. Accompanied with propeptide-shortening, the pro-mature junction became more susceptible toward the maturation enzymes. We demonstrated the in vitro Glu-specific endopeptidase activity of exfoliative toxin (ET) A for the first time, which was measured with Escherichia coli-expressed recombinant ETAs and synthetic peptidyl substrates. The animal model revealed that the proteolytic activity was indispensable for exfoliation of the skin. In addition, we determined characteristics of DPP11 and DPP7, and proposed a novel phylogenetic system of these family molecules.