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CHOK1 cells that express an α4/GFP chimera as well as endogenous α5β1 integrin (CHO-α4/GFP), also bound to the ADAM12 disintegrin domain, and this interaction was disrupted by the anti-α4 antibody (Figure 1C). Binding of CHOB2-α4 cells was inhibited by an antibody against the α4, but not one against the α5, integrin subunit (Figure 1A). In contrast, CHOB2-α5 cells, which express the human α5 integrin and bind to fibronectin (FN) (Figure 1B), did not adhere to the ADAM12 disintegrin domain (Figure 1A). As seen in Figure 1A, CHOB2 cells that express the human α4 integrin subunit (CHOB2-α4), bound to a recombinant ADAM12 disintegrin domain. We also tested whether cells expressing α5β1 integrin adhere because we are interested in the selectivity of ADAM-integrin interactions, and because very few ADAM disintegrin domains have been reported to interact with α5β1 integrin (White et al., 2005).
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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. To assess whether the D488A mutant is a less potent inhibitor of α4β1-mediated cell migration (Figure 5B) because it is not processed (Figure 6A), we set out to generate an “unprocessed” ADAM12. As seen in Figure 5B, the mutant D488A was compromised in its ability to inhibit α4β1-mediated cell migration compared with wild-type ADAM12. We therefore tested the effects of full-length ADAM12 containing the D488A mutation on α4β1-mediated cell migration. Expression of ADAM12 had no significant effect on the migration of Chinese hamster ovary (CHO) cells expressing α5β1 integrin on FN, as assessed using transwell (Figure 2, E and G) and scratch wound (Figure 2, F and H) assays. ADAM12 inhibits migration of α4β1- but not α5β1 integrin-expressing cells on fibronectin.
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