Regulatory role of ginsenoside Rp1, a novel ginsenoside derivative, on CD29-mediated cell adhesion.
In this study, we examined the regulatory role of G-Rp1 on cell adhesion events mediated by beta1-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.
Kim
Byung Hun
BH
School of Bioscience and Biotechnology, Kangwon National University, Chuncheon, Korea.
Cho
Jae Youl
JY
D002448:Cell Adhesion / Q000187:drug effects* / Q000502:physiology; D015815:Cell Adhesion Molecules / Q000378:metabolism; D003571:Cytochalasin B / Q000494:pharmacology; D036145:Ginsenosides / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D019012:Integrin beta1 / Q000378:metabolism*; D015394:Molecular Structure; D011494:Protein Kinases / Q000378:metabolism; D020298:U937 Cells
D015815:Cell Adhesion Molecules; D036145:Ginsenosides; D019012:Integrin beta1; C512675:ginsenoside Rp1; D003571:Cytochalasin B; D011494:Protein Kinases