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CHOB2-α5 and CHOK1 cells (provided by A. Rick Horwitz, University of Virginia) were maintained in DMEM containing 10% fetal bovine serum (FBS) (Invitrogen), l-glutamine, nonessential amino acids, and antibiotics. The α5β1 integrin engages the central cell binding domain (CCBD) of FN and forms focal adhesions, which function both as anchors and as signaling centers. In particular, the fibronectin (FN) binding integrins α4β1 and α5β1 are well characterized for their roles in cell motility. Although it is recognized that recombinant ADAM disintegrin domains can interact with integrins, little is known about ADAM-integrin interactions in cellular context.
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(C and D) CHO-α4/GFP (black) and CHOK1 cells (white) were pretreated with either no antibody or 5 μg/ml anti-α4 antibody (HP2/1) for 30 min before adding to wells coated with 5 μg/ml ADAM12 disintegrin domain (C) or human plasma FN (D). These observations indicate that cells can adhere to a recombinant ADAM12 disintegrin domain using the α4β1 but not the α5β1 integrin. Parental CHOK1 cells, which express endogenous α5β1 integrin and which bind to FN (Figure 1D), did not adhere to the ADAM12 disintegrin domain (Figure 1C). 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).
