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Full-length ADAM12 inhibits the migration of CHO-α4/GFP cells on the α4β1 binding CS-1 region but not on the α5β1 binding CCBD of fibronectin. In contrast, expression of ADAM12 had no significant effect on the migration of the same cells (CHO-α4/GFP) on the α5β1 substrate (Figure 3C). For each experiment, the average migration rate of ADAM12-transfected cells was normalized to that of mock-transfected cells.
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Like ADAM12, ADAM19 and 33 are expressed at the surface of CHO cells in both pro- and metalloprotease active (Met) forms (Figure 6D). We extended our analysis to ADAM19 and ADAM33, two other ADAMs that are phylogenetically related to Xenopus ADAM13 and that are found in mouse cranial neural crest cells (Tomczuk, 2004). CHO-α4GFP cells transiently expressing ADAM12, ADAM17, ADAM19, or ADAM33 were compared for their relative ability to inhibit wound closure after 12 h on the CS-1 region of FN. In contrast, although some of the ADAM12-transfected cells extended membrane protrusions, these protrusions were less robust and did not lead to effective cell body translocation (Movie 2B).
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Analysis of movies showed that mock transfected cells displayed broad lamellipodia at the leading edge and the cells moved persistently in the direction of the protrusion (Movie 2A). In contrast, both the rate (Figure 7C) and persistence (Figure 7D) of migration of ADAM12-transfected cells were reduced and the cells showed little net translocation (Figure 7B). We also assessed the effect of expressing ADAM12 on random cell migration on the CS-1 region of FN. Collectively, the results of Figures 5 and 6 show that the inhibitory effect of ADAM12 on α4β1-mediated cell migration does not require that it be proteolytically processed nor that it be proteolytically active. We then tested the poorly processed (SGAA) and catalytic site (E/A) mutants for their effects on α4β1-mediated cell migration in scratch wound assays on the CS-1 region of FN.
