Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains

被引:129
作者
Annabi, B
Lachambre, MP
Bousquet-Gagnon, N
Pagé, M
Gingras, D
Béliveau, R
机构
[1] Hop St Justine, Mol Med Lab, Montreal, PQ H3C 3P8, Canada
[2] Univ Quebec, Montreal, PQ H3C 3P8, Canada
关键词
angiogenesis; cancer; caveolin; cell migration; glioblastoma;
D O I
10.1042/0264-6021:3530547
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a membrane-associated MMP that has been recently reported to have a central role in tumour cell invasion. Here we report that both the native and overexpressed recombinant forms of MT1-MMP are highly enriched in low-density Triton X-100-insoluble membrane domains that contain the caveolar marker protein caveolin 1. Moreover, the MT1-MMP-dependent activation of proMMP-2 induced by concanavalin A and cytochalasin D was correlated with the processing of MT1-MMP to its proteolytically inactive 43 kDa fragment in U-87 glioblastoma and MT-1080 fibrosarcoma tumour cell lines: this processing was also preferentially observed within the caveolar fraction. Interestingly, whereas the expression of caveolin 1 had no effect on the MT1-MMP-dependent activation of proMMP-2, its co-expression with MT1-MMP antagonized the MT1-MMP-increased migratory potential of COS-7 cells. Taken together, our results provide evidence that MT1-MMP is preferentially compartmentalized and proteolytically processed in caveolae of cancer cells. The inhibition of MT1-MMP-dependent cell migration by caveolin 1 also suggests that the localization of MT1-MMP to caveolin-enriched domains might have an important function in the control of its enzymic activity.
引用
收藏
页码:547 / 553
页数:7
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