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- W2054927341 abstract "In this study, we examined the regulatory role of G-Rp1 on cell adhesion events mediated by β1-integrins (CD29). Using a U937 cell-cell adhesion assay, we found that exogenous G-Rp1 down-regulates CD29 activation in a dose-dependent manner, whereas G-Rg3 did not cause the same effect. However, G-Rp1 increased cell-fibronectin adhesion comparable to cytochalasin B, an actin cytoskeleton disruptor. Furthermore, G-Rp1 also blocked the rearrangement of actin at sites of cell-cell contact, indicating that the actin cytoskeleton may be a target of G-Rp1 action. Interestingly, G-Rp1 suppressed dephosphorylation of vasodilator-stimulated phosphoprotein (VASP) at Ser-157, known to be an actin cytoskeleton modulatory protein. These results suggest that G-Rp1 may act as a novel regulator of CD29-mediated cell adhesion events, which are involved in numerous pathological symptoms." @default.
- W2054927341 created "2016-06-24" @default.
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- W2054927341 date "2009-01-22" @default.
- W2054927341 modified "2023-09-26" @default.
- W2054927341 title "Regulatory Role of Ginsenoside Rp1, a Novel Ginsenoside Derivative, on CD29-Mediated Cell Adhesion" @default.
- W2054927341 doi "https://doi.org/10.1055/s-0028-1112213" @default.
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