Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members

Pinco Casino delivers a polished lobby packed with hit titles, engaging features, and generous promotions tailored for slot lovers. This work was supported by National Institutes of Health Grant GM (to J.M.W.). Further studies will investigate the mechanisms and consequences of this newly appreciated ADAM function. In contrast, as noted above, the disintegrin domain seems to be important for this activity.

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Cells were either mock transfected or transfected to express full-length ADAM12, and transwell migration assays (A, C, E, and G) or scratch wound assays (B, D, F, and H) were conducted 24 h after transfection. Cells expressing α4β1 but not α5β1 integrin bind to recombinant ADAM12 disintegrin domain. A previous study demonstrated that GFP-tagged α4 integrin behaves like untagged α4 integrin (Pinco et al., 2002). Transwell migration assays were performed as described previously (Liu et al., 1999), with the following modifications. After incubation for 2 h in a CO2 incubator at 37°C, confluent cell monolayer was scraped with a yellow Pipetman tip to generate scratch wounds. Scratch wound migration assays were performed as described previously (Pinco et al., 2002).

Possible Mechanisms by Which ADAMs Influence Integrin-mediated Cell Migration

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