Comparative study on the cell toxicity and enzymatic activity of two northern scyphozoan species Cyanea capillata (L.) and Cyanea lamarckii (Péron & Léslieur)

Toxicon. 2007 Jul;50(1):53-64. doi: 10.1016/j.toxicon.2007.02.014. Epub 2007 Mar 6.

Abstract

Two species of venomous pelagic cnidaria are compared according to their enzymatic, cytotoxic and haemolytic potency. The widely distributed jellyfish Cyanea capillata and Cyanea lamarckii were collected in the North Sea at the coasts of the Orkney Island and the Island of Helgoland. Purified cnidocyst extracts from fishing and mesenteric tentacles were prepared and tested for their bioactivity. The haemolysis induced by toxins of C. capillata was determined with respect to organism size and toxigenic organs. The haemolytic activity of the related species C. lamarckii was documented for the first time. Dose dependent haemolytic activities have been detected by means of protein equivalents at concentrations above 20mug(protein)/mL. Extracts of fishing tentacle cnidocysts showed a less potent haemolytic activity compared to extracts of mesenteric tentacles. In vitro studies with permanent cells of a hepatoma cell line have shown a time and concentration dependent loss of cell vitality up to 90% at 33.3mug(protein)/mL (10mug(protein)/10(5) cells). Supplementing the cell based toxicity tests an enzyme assay was performed to measure a phospholipase A(2) (PLA(2)) activity. A PLA(2)-like activity could be demonstrated in cnidocysts extracts prepared from mesenteric and fishing tentacles of both jellyfish species.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Cell Line, Tumor
  • Cell Survival
  • Cnidaria / cytology
  • Cnidaria / enzymology*
  • Cnidaria / metabolism
  • Cnidarian Venoms / enzymology*
  • Cnidarian Venoms / isolation & purification
  • Cnidarian Venoms / toxicity*
  • Erythrocytes
  • Hemolysis
  • Humans
  • North Sea
  • Phospholipases A2 / metabolism
  • Statistics, Nonparametric

Substances

  • Cnidarian Venoms
  • Phospholipases A2