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Further genetic experiments suggested that UNC-71 acts together with integrins for proper axon guidance (Huang et al., 2003). We studied ADAMs 12, 19, and 33 because they are phylogenetically related to an ADAM (Xenopus ADAM13) that functions in Xenopus cranial neural crest migration (Alfandari et al., 2001), and because they are expressed in mouse cranial neural crest (Tomczuk, 2004). We first extended our analysis to ADAM17 (tumor necrosis factor-α converting enzyme), an important ADAM that was recently shown to interact with the α5β1 integrin (Bax et al., 2004). As seen in Figure 5B, both the poorly processed (SGAA) and the protease dead (E/A) mutants inhibited migration as much as wild-type ADAM12. As seen in Figure 6C, E/A ADAM12 was transported to the cell surface and processed as well as wild-type ADAM12.
ADAM12 disintegrin loop mutants (R481A, D488A, and E491A), were generated using a site-directed mutagenesis kit (Stratagene), using the 6XHis-tagged ADAM12 disintegrin domain as the template. To produce protein with higher purity, a 6Xhistidine (His) tag was added to the 3′ end of the disintegrin domain coding sequence, using a site-directed mutagenesis kit (Stratagene, La Jolla, CA). Mouse ADAM12 disintegrin domain in the vector pGEX-2T was provided by Anna Zolkiewski (Kansas State University, Manhattan, KS). Mouse anti-α4 integrin functional blocking monoclonal antibody (mAb) HP2/1 and mouse anti-α5 integrin functional blocking antibody CBL497 were obtained from Chemicon International (Temecula, CA).
ADAM12 Inhibits Integrin α4β1-mediated Random Cell Motility
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We thank many colleagues for gifts of cells and plasmids as noted in Materials and Methods. Although ADAM12 expression can moderately increase cell adhesion to FN or FN fragments, this effect is not specific to α4β1 integrin (Huang and White, unpublished data). 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).