Molecular basis for the control of intractable diseases through manipulation of osteopontin function.

已经表明，隐藏表位S162 VVYGLR 168通过凝血酶切割人骨桥蛋白（OPN）而暴露，并且该表位被α 4和α 9整联蛋白识别。1）我们发现V164、Y105和L167残基对于α 9和α 4整联蛋白在细胞粘附和迁移方面的识别是关键的。同时，R168残基是α 9整合素在细胞粘附中识别的关键，V163是α 4整合素在细胞迁移中识别的关键。2）我们还发现，当SVVYGLR被α 4和α 9整合素识别时，R168残基传递了Rho介导的功能的负信号。3）OPN也在SVVYG 166和α 9整合素的位置被MMP-3和MMP-7切割。L167R我们发现α 4整合素，而不是α 9整合素能够识别MMP切割的OPN。

It has been shown that the cryptic epitope, S162VVYGLR168, is exposed by the cleavage of human osteopontin (OPN) by thrombin and this epitope is recognized by a 4 and a 9 integrins.1) We found that V164, Y105 and L167 residues are critical for the recognition by both a 9 and a 4 integrins in terms of cell adhesion and migration. While, R168 residue is critical for the recognition by a 9 integrin in cell adhesion and V163 is important for a 4 integrin in cell migration.2) We also found that R168 residue transmits negative signal for Rho mediated-function when SVVYGLR is recognize by a 4 and a 9 integrins in cell migration.3) OPN is also cleaved by MMP-3 and MMP-7 at a position of SVVYG166/L167R. We found that a 4 integrin, but not a 9 integrin is able to recognized MMP-cleaved from of OPN.