Modulation of protein kinase C activity in NIH 313 cells by plant glycosides from Panax ginseng
- Authors
- Byun, Boo Hyeong; Shin, Incheol; Yoon, Yoo-Sik; Kim, Shin Il; Joe, Cheol O.
- Issue Date
- Oct-1997
- Publisher
- GEORG THIEME VERLAG KG
- Keywords
- Panax ginseng; araliaceae; ginsenoside; phospholipase C; protein kinase C; myristoylated alanine-rich C kinase substrate
- Citation
- PLANTA MEDICA, v.63, no.5, pp 389 - 392
- Pages
- 4
- Journal Title
- PLANTA MEDICA
- Volume
- 63
- Number
- 5
- Start Page
- 389
- End Page
- 392
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/67072
- DOI
- 10.1055/s-2006-957719
- ISSN
- 0032-0943
1439-0221
- Abstract
- The involvement of ginsenosides in the signal cascade that stimulates cellular growth was investigated. It was found that ginsenosides Rh-1 and Rh-2 extracted from the root of Panax ginseng inhibited cellular proliferation in NIH 3T3 fibroblasts. Both ginsenosides Rh-1 and Rh-2 effectively reduced phospholipase C activity resulting in a decrease in the intracellular level of diacylglycerol, an endogenous activator of protein kinase C. The treatment of cells with Rh-1 or Rh-2 was thus found to reduce intracellular protein Itinase C activity. We also observed that the phosphorylation of myristoylated alanine-rich C kinase substrate, one of the major substrates of protein Itinase C in cells, was inhibited by the ginsenosides. Data suggest that the ginsenoside Rh-1 or Rh-2 exerts antiproliferative effects by inhibiting phospholipase C, which produces second messengers necessary for the activation of protein kinase C.
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