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Titolo:
MODULATION OF PROTEIN-KINASE-C ACTIVITY IN NIH-313 CELLS BY PLANT GLYCOSIDES FROM PANAX-GINSENG
Autore:
BYUN BH; SHIN I; YOON YS; KIM SI; JOE CO;
Indirizzi:
KOREA ADV INST SCI & TECHNOL,DEPT BIOL SCI TAEJON 305701 SOUTH KOREA KOREA ADV INST SCI & TECHNOL,DEPT BIOL SCI TAEJON 305701 SOUTH KOREA KYUNGSAN UNIV,DEPT ORIENTAL MED KYUNGSAN 712240 SOUTH KOREA KOREA GINSENG & TOBACCO RES INST TAEJON 305345 SOUTH KOREA
Titolo Testata:
Planta medica
fascicolo: 5, volume: 63, anno: 1997,
pagine: 389 - 392
SICI:
0032-0943(1997)63:5<389:MOPAIN>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHORYLATION; INHIBITION; CALMODULIN; SUBSTRATE; METABOLISM; INVITRO; MARCKS; PHOSPHATIDYLINOSITOL; TRANSFORMATION; INCREASES;
Keywords:
PANAX GINSENG; ARALIACEAE; GINSENOSIDE; PHOSPHOLIPASE C; PROTEIN KINASE C; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
B.H. Byun et al., "MODULATION OF PROTEIN-KINASE-C ACTIVITY IN NIH-313 CELLS BY PLANT GLYCOSIDES FROM PANAX-GINSENG", Planta medica, 63(5), 1997, pp. 389-392

Abstract

The involvement of ginsenosides in the signal cascade that stimulatescellular growth was investigated. It was found that ginsenosides Rh-1and 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 20:24:31