Fosang A J, Last K, Fujii Y, Seiki M, Okada Y
Orthopaedic Molecular Biology Research Unit, Melbourne University, Royal Children's Hospital, Parkville, Australia.
FEBS Lett. 1998 Jul 3;430(3):186-90. doi: 10.1016/s0014-5793(98)00667-x.
An aggrecan G1-G2 substrate was used to determine sites within the interglobular domain that were susceptible to cleavage by MT1-MMP. Degradation products were identified by Western blotting with neo-epitope antibodies specific for MMP-derived N- and C-terminal sequences. The results showed that MT1-MMP cleaved at the N341-F342 and D441-L442 bonds, as shown for other MMPs, and also at a site 13 amino acids C-terminal to the N341-F342 site. The G2 product of this additional cleavage was identified by sequence analysis and revealed an N-terminus commencing T355VxxPDVELPLP. The data are consistent with MT1-MMP cleavage at three sites in the aggrecan interglobular domain; one at N342-F342, a second at D441-L442 and a third at Q354-T355.
使用聚集蛋白聚糖G1-G2底物来确定球状结构域内易被MT1-MMP切割的位点。通过用对MMP衍生的N端和C端序列具有特异性的新表位抗体进行蛋白质印迹法来鉴定降解产物。结果表明，MT1-MMP如其他MMP一样在N341-F342和D441-L442键处切割，并且还在N341-F342位点C端13个氨基酸处的一个位点切割。通过序列分析鉴定了这种额外切割的G2产物，其N端起始于T355VxxPDVELPLP。这些数据与MT1-MMP在聚集蛋白聚糖球状结构域的三个位点切割一致；一个在N342-F342，第二个在D441-L442，第三个在Q354-T355。
