Department of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi 467-8603, Japan.
Biol Pharm Bull. 2010;33(6):1047-9. doi: 10.1248/bpb.33.1047.
Reelin is a very large secreted glycoprotein that is essential for brain formation and function, but the mechanism by which it affects the dynamics and morphology of neuronal cells remains unsolved. One previous study claimed that Reelin has a proteolytic activity against extracellular matrix proteins, which might explain many of the actions of Reelin. Therefore, in this study wild-type Reelin protein and its mutant in which a supposedly critical serine residue was replaced were expressed and tested for their self-degrading and laminin-degrading activities. We found that both of these proteins generated totally the same cleaved fragments and that neither of them is capable of degrading laminin. It is thus likely that Reelin is not a serine protease and is unable to degrade extracellular matrix.
瑞林是一种非常大的分泌糖蛋白,对大脑的形成和功能至关重要,但它影响神经元细胞动态和形态的机制尚不清楚。之前有一项研究声称,瑞林对细胞外基质蛋白具有蛋白水解活性,这可能解释了瑞林的许多作用。因此,在这项研究中,野生型瑞林蛋白及其突变体(一个假定的关键丝氨酸残基被替换)被表达并测试其自我降解和层粘连蛋白降解活性。我们发现这两种蛋白都产生了完全相同的裂解片段,而且它们都不能降解层粘连蛋白。因此,瑞林可能不是丝氨酸蛋白酶,也不能降解细胞外基质。