Journal
PLANTA MEDICA
Volume 75, Issue 4, Pages 316-320Publisher
GEORG THIEME VERLAG KG
DOI: 10.1055/s-0028-1112213
Keywords
ginsenoside Rp1; beta 1-integrin-mediated cell adhesion; actin cytoskeleton; VASP
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Funding
- KRF, Korea [KRF-2006-311-C00455]
- National Research Foundation of Korea [2006-311-C00455] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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In this study, we examined the regulatory role of G-Rp1 on cell adhesion events mediated by beta 1-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.
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