• Title/Summary/Keyword: Giant jellyfish

Search Result 12, Processing Time 0.018 seconds

New Alkoxyglycerols from the Jellyfish Nemopilema nomurai

  • Liu, Ju-An;Li, Fa-Mei;Hong, Jong-Ki;Kim, Eun-La;Yoo, Eun-Sook;Kim, Eui-Kyung;Yoon, Won-Duk;Jung, Jee-H.
    • Natural Product Sciences
    • /
    • v.15 no.2
    • /
    • pp.71-75
    • /
    • 2009
  • The great economic and social damage caused by unusual explosion of jellyfish population has attracted the attention of researchers. A chemical study on the bioactive components of the giant jellyfish Nemopilema nomurai led to the isolation of two new (1 and 2) and three known alkoxyglycerols (3 - 5), along with known monoglycerides (6 - 7) and fatty acids. Based on NMR and MS data, the structures of compounds 1 and 2 were elucidated as 1-O-[(Z)-tetradec-3-enyl]-sn-glycerol and 1-O-[(Z)-octadec-10-enyl]-sn-glycerol, respectively. The absolute configurations of compounds 1 - 7 were determined by comparison of specific optical rotation values with those reported. The isolated compounds were evaluated for suppressive effect on the proinflammatory mediators (NO, IL-6, and TNF-${\alpha}$) in murine macrophage cells. However, they were found inactive upto the concentration of 100 ${\mu}M$.

Viriditoxin Induces G2/M Cell Cycle Arrest and Apoptosis in A549 Human Lung Cancer Cells

  • Park, Ju Hee;Noh, Tae Hwan;Wang, Haibo;Kim, Nam Deuk;Jung, Jee H.
    • Natural Product Sciences
    • /
    • v.21 no.4
    • /
    • pp.282-288
    • /
    • 2015
  • Viriditoxin is a fungal metabolite isolated from Paecilomyces variotii, which was derived from the giant jellyfish Nemopilema nomurai. Viriditoxin was reported to inhibit polymerization of FtsZ, which is a key protein for bacterial cell division and a structural homologue of eukaryotic tubulin. Both tubulin and FtsZ contain a GTP-binding domain, have GTPase activity, assemble into protofilaments, two-dimensional sheets, and protofilament rings, and share substantial structural identities. Accordingly, we hypothesized that viriditoxin may inhibit eukaryotic cell division by inhibiting tubulin polymerization as in the case of bacterial FtsZ inhibition. Docking simulation of viriditoxin to ${\beta}-tubulin$ indicated that it binds to the paclitaxel-binding domain and makes hydrogen bonds with Thr276 and Gly370 in the same manner as paclitaxel. Viriditoxin suppressed growth of A549 human lung cancer cells, and inhibited cell division with G2/M cell cycle arrest, leading to apoptotic cell death.