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Our results indicate that distinct ADAMs can modulate cell migration mediated by specific integrins in a pattern dictated, at least in part, by their disintegrin domains. A point mutation in the ADAM12 disintegrin loop partially reduced the inhibitory effect of ADAM12 on cell migration on the α4β1 binding fragment of fibronectin, whereas mutations that block metalloprotease activity had no effect. We found that ADAMs inhibit integrin-mediated cell migration in patterns dictated by the integrin binding profiles of their isolated disintegrin domains.
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As seen in Figure 6C, E/A ADAM12 was transported to the cell surface and processed as well as wild-type ADAM12. The molecular weights of these ADAM constructs reflect the presence of the 6Xmyc tag appended at the C terminus of each construct. Wild-type and the disintegrin loop (D488A) ADAM12 (A); wild-type ADAM12 and ADAM12 with mutations in the putative furin cleavage sites (B); wild-type and E/A (protease inactive) ADAM12 (C); and wild-type ADAMs 12, 17, 19, and 33 (D). A biochemical analysis revealed, to our surprise, that although D488A ADAM12 is expressed and transported to the cell surface, it is not proteolytically processed (Figure 6A). As seen in Table 1, expression of ADAM12 did not change either the total or the surface levels of the α4 integrin subunit. In contrast, lamellipodia protrusions and cell body translocation seemed less robust in ADAM12 transfected samples (Figure 4B, right, and Movie 1B).
