Reference : Contribution of MT1-MMP and of Human Laminin-5 Gamma2 Chain Degradation to Mammary Ep...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/10445
Contribution of MT1-MMP and of Human Laminin-5 Gamma2 Chain Degradation to Mammary Epithelial Cell Migration
English
Gilles, Christine mailto [Université de Liège - ULiège > Département des sciences cliniques > Labo de biologie des tumeurs et du développement >]
Polette, M. [> > > >]
Coraux, C. [> > > >]
Tournier, J. M. [> > > >]
Meneguzzi, G. [> > > >]
Munaut, Carine mailto [Université de Liège - ULiège > Département des sciences cliniques > Labo de biologie des tumeurs et du développement >]
Volders, Laure [Centre Hospitalier Universitaire de Liège - CHU > > Agents détachés à l'Université (Site Sart Tilman) >]
Rousselle, P. [> > > >]
Birembaut, P. [> > > >]
Foidart, Jean-Michel mailto [Université de Liège - ULiège > Département des sciences cliniques > Gynécologie - Obstétrique >]
Aug-2001
Journal of Cell Science
Company of Biologists
114
Pt 16
2967-76
Yes (verified by ORBi)
International
0021-9533
1477-9137
Cambridge
United Kingdom
[en] Membrane-type matrix metalloproteinase 1 (MT1-MMP) is a membrane-anchored matrix metalloproteinase (MMP) that is frequently associated with processes involving tissue remodelling and cell migration. We have examined MT1-MMP expression and subcellular distribution as a function of MCF10A mammary epithelial cell migration using an in vitro outgrowth migration assay. Stronger expression of MT1-MMP was observed at the mRNA and at the protein level in cells at the periphery of the outgrowth. As shown by videomicroscopy, these cells were involved in an orientated cell migration, in contrast to stationary cells distant from the periphery. Furthermore, MT1-MMP was mainly distributed in lamellipodia of migratory cells, as well as at their basal surface in contact with the substrate. Laminin-5 (Ln-5), a recently described substrate for MT1-MMP, was deposited preferentially in the matrix by migratory cells. Fragments of the gamma2 subunit of Ln-5 were also identified in migratory cultures of MCF10A cells, attesting to its proteolytic degradation. These fragments corresponded in size to those we observed after incubation of purified human Ln-5 with the recombinant catalytic domain of human MT1-MMP. We also show that anti-Ln5 blocking antibodies, MMP inhibitors (BB94 and TIMP-2) and MT1-MMP antisense oligonucleotides significantly decreased MCF10A cell migration. Taken together, these observations demonstrate that MT1-MMP is spatially and temporally regulated during MCF10A cell migration, and suggest that MT1-MMP-mediated pericellular proteolysis of Ln-5 gamma2 chain could contribute to this process.
http://hdl.handle.net/2268/10445

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