Please use this identifier to cite or link to this item: http://hdl.handle.net/1893/17904
Appears in Collections:Biological and Environmental Sciences Journal Articles
Peer Review Status: Refereed
Title: A putative link between phagocytosis-induced apoptosis and hemocyanin-derived phenoloxidase activation
Authors: Coates, Christopher
Whalley, Tim
Wyman, Michael
Nairn, Jacqueline
Contact Email: jacqueline.nairn@stir.ac.uk
Keywords: Phosphatidylserine
Apoptosis
Phagocytosis
Innate immunity
Limulus polyphemus
Damage-associated patterns
Issue Date: Nov-2013
Publisher: Springer
Citation: Coates C, Whalley T, Wyman M & Nairn J (2013) A putative link between phagocytosis-induced apoptosis and hemocyanin-derived phenoloxidase activation, Apoptosis, 18 (11), pp. 1319-1331.
Abstract: Apoptosis and phagocytosis are crucial processes required for developmental morphogenesis, pathogen deterrence and immunomodulation in metazoans. We present data showing that amebocytes of the chelicerate, Limulus polyphemus, undergo phagocytosis-induced cell death after ingesting spores of the fungus, Beauveria bassiana, in vitro. The observed biochemical and morphological modifications associated with dying amebocytes are congruent with the hallmarks of apoptosis, including: extracellularisation of phosphatidylserine, intranucleosomal DNA fragmentation and an increase in caspase 3/7-like activities. Previous studies have demonstrated that phosphatidylserine is a putative endogenous activator of hemocyanin-derived phenoloxidase, inducing conformational changes that permit phenolic substrate access to the active site. Here, we observed extracellular hemocyanin-derived phenoloxidase activity levels increase in the presence of apoptotic amebocytes. Enzyme activity induced by phosphatidylserine or apoptotic amebocytes was reduced completely upon incubation with the phosphatidylserine binding protein, annexin V. We propose that phosphatidylserine redistributed to the outer plasma membrane of amebocytes undergoing phagocytosis-induced apoptosis could interact with hemocyanin, thus facilitating its conversion into a phenoloxidase-like enzyme, during immune challenge.
Type: Journal Article
URI: http://hdl.handle.net/1893/17904
DOI Link: http://dx.doi.org/10.1007/s10495-013-0891-x
Rights: The publisher does not allow this work to be made publicly available in this Repository. Please use the Request a Copy feature at the foot of the Repository record to request a copy directly from the author. You can only request a copy if you wish to use this work for your own research or private study.
Affiliation: Biological and Environmental Sciences
Biological and Environmental Sciences
Biological and Environmental Sciences
Biological and Environmental Sciences

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