In vitro phenoloxidase activity in the blood of Ciona intestinalis and other ascidians.
The presence and activation of phenoloxidase in the blood of Ciona intestinalis and other ascidians was investigated in vitro. In C. intestinalis, phenoloxidase was found to exist in the cells as a proenzyme and to be activated by proteases. The microbial carbohydrates, LPS or laminarin, also enhanced enzyme activity but a similar effect was not achieved with other sugars. Calcium was not essential for enzyme activity and no enzyme suppression was seen at high calcium concentrations. Prophenoloxidase activation by LPS was further found to be dose related and inhibited by PTU and tropolone. Since benzamidine and STI reduced phenoloxidase activity in cell lysate supernatants, activation may involve other factors, possibly a serine protease. Lastly, as phenoloxidase activity was detected in the blood cells (usually the morula cells) of eight other ascidian species, it appears that it is widely distributed in the blood of this group of invertebrates.
Department of Biology and Preclinical Medicine, Gatty Marine Laboratory, University of St Andrews, Fife, Scotland.
A D
AD
Jackson
V J
VJ
Smith
C M
CM
Peddie
D000818:Animals; D001773:Blood Cells / Q000201:enzymology; D002118:Calcium / Q000494:pharmacology; D002938:Ciona intestinalis / Q000201:enzymology*; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation / Q000187:drug effects; D008070:Lipopolysaccharides / Q000494:pharmacology; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors / Q000097:blood*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013045:Species Specificity; D014561:Urochordata / Q000201:enzymology
D008070:Lipopolysaccharides; D015842:Serine Proteinase Inhibitors; D014442:Monophenol Monooxygenase; D002118:Calcium