Cytoplasmic salt bridge formation in integrin αvß3 stabilizes its inactive state affecting integrin-mediated cell biological effects

Alternative splicing of KAI1 abrogates its tumor-suppressive effects on integrin αvβ3-mediated ovarian cancer biology

“…Adhesion data from cells attached to uncoated cell culture dishes did not reach significance levels when compared to the respective vector transfectants. [51,52]. Vector transfectants (vec) or OV-MZ-6-WT cells (wt) with low endogenous αvβ3 levels served as controls.…”

“…Immunocytochemical analysis of p-FAK expression in the presence of KAI1-WT or KAI1-SP. Staining of p-FAK was conducted as described [51,52]. Representative fluorescence images are illustrated together with the corresponding differential interference contrast images.…”

“…Immunocytochemical staining of cellular p-FAK (Y397) was conducted as previously outlined [51,52]. Staining procedures in the absence of any Ab or in the presence of the secondary Ab alone did not result in noticeable fluorescence signals.…”

“…Cell proliferative activity of KAI1-WT-or KAI1-SP-transfected OV-MZ-6-WT cells as well as control vector transfectants and OV-MZ-6-WT (wt) was determined by MTT assays as described earlier[51,52]. Data from four independent experiments are depicted as "n-fold" (± s.d.)…”

Emergence of Small-Molecule Non-RGD-Mimetic Inhibitors for RGD Integrins

“…10,11 The conformational changes can be caused by Òinside-outÓ signaling, during which proteins within the cell, such as talin and kindlins, bind to the transmembrane base of the β domain and induce the change in conformation outside the cell by disrupting the salt bridge. 1,[11][12][13] Alternatively, Òoutside-inÓ signaling can also result in conformational changes when the integrin ectodomain interacts with a ligand, allowing the cell to sense and react to the extracellular environment. 12,16 and Tyr122 of the β 3 subdomain may be central to interacting with the inactive integrin without inducing any conformational changes in the receptor.…”