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DOI: 10.1055/s-0028-1112213
© Georg Thieme Verlag KG Stuttgart · New York
Regulatory Role of Ginsenoside Rp1, a Novel Ginsenoside Derivative, on CD29-Mediated Cell Adhesion
Publication History
Received: September 27, 2008
Revised: November 4, 2008
Accepted: November 10, 2008
Publication Date:
22 January 2009 (online)
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.
Key words
ginsenoside Rp1 - β1-integrin-mediated cell adhesion - actin cytoskeleton - VASP
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Jae Youl Cho, PhD
School of Bioscience and Biotechnology and
Institute of Bioscience and Biotechnology
Kangwon National University
Chuncheon 200–701
Korea
Phone: +82-33-250-6488
Fax: +82-33-253-6560
Email: jaecho@kangwon.ac.kr
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