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Activation of protein kinase C by phorbol esters disrupts the tegument of Schistosoma mansoni

Published online by Cambridge University Press:  06 April 2009

P. M. Wiest
Affiliation:
Division of Geographic Medicine, The Department of Medicine, The Miriam Hospital and The International Health Institute, Brown University and Division of Biology and Medicine, Brown University, Providence, RI 02906, USA
S. S. Kunz
Affiliation:
Division of Geographic Medicine, The Department of Medicine, The Miriam Hospital and The International Health Institute, Brown University and Division of Biology and Medicine, Brown University, Providence, RI 02906, USA
K. R. Miller
Affiliation:
Division of Geographic Medicine, The Department of Medicine, The Miriam Hospital and The International Health Institute, Brown University and Division of Biology and Medicine, Brown University, Providence, RI 02906, USA

Summary

The tegument of the human parasite Schistosoma mansoni is critical for parasite survival within the mammalian host. The role of protein kinase C (PKC), a major effector molecule in the phosphoinositide pathway, in maintaining the structural organization of this syncytial layer was examined in adult worms. Phorbol 12-myristate, 13-acetate (PMA) and phorbol 12,13-dibutyrate (PDB), phorbol esters that activate PKC, induced formation of surface vesicles as determined by light and scanning electron microscopy. Similar results were seen with sn-2-dioctanoyl-glycerol, a synthetic analogue of diacylglycerol. No effect was seen in parasites incubated with 4-a-phorbol ester or a isomers of PMA or PDB, compounds that do not activate PKC. Vesicle formation was reversible in parasites treated with sn-2-dioctanoyl-glycerol but not with phorbol esters. The tegument of male worms was more sensitive to the effect of phorbol esters than females. Transmission electron microscopy revealed vacuolization of the tegument. These data suggest that signal transduction pathways may have a critical role in the maintenance of the structural integrity of the tegument of parasitic helminths.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1994

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