Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica

The enteric protozoan parasite Entamoeba histolytica is the causative agent of human amebiasis. During infection, adherence of E. histolytica through Gal/GalNAc lectin on the surface of the amoeba can induce caspase-3-dependent or -independent host cell death. Phosphorylinositol 3-kinase (PI3K) and...

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Main Authors: Lee, Young Ah, Kim, Kyeong Ah, Min, Arim, Shin, Myeong Heon
Format: Online
Language:English
Published: The Korean Society for Parasitology and Tropical Medicine 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4170031/
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recordtype oai_dc
spelling pubmed-41700312014-09-22 Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica Lee, Young Ah Kim, Kyeong Ah Min, Arim Shin, Myeong Heon Original Article The enteric protozoan parasite Entamoeba histolytica is the causative agent of human amebiasis. During infection, adherence of E. histolytica through Gal/GalNAc lectin on the surface of the amoeba can induce caspase-3-dependent or -independent host cell death. Phosphorylinositol 3-kinase (PI3K) and protein kinase C (PKC) in E. histolytica play an important function in the adhesion, killing, or phagocytosis of target cells. In this study, we examined the role of amoebic PI3K and PKC in amoeba-induced apoptotic cell death in Jurkat T cells. When Jurkat T cells were incubated with E. histolytica trophozoites, phosphatidylserine (PS) externalization and DNA fragmentation in Jurkat cells were markedly increased compared to those of cells incubated with medium alone. However, when amoebae were pretreated with a PI3K inhibitor, wortmannin before being incubated with E. histolytica, E. histolytica-induced PS externalization and DNA fragmentation in Jurkat cells were significantly reduced compared to results for amoebae pretreated with DMSO. In addition, pretreatment of amoebae with a PKC inhibitor, staurosporine strongly inhibited Jurkat T cell death. However, E. histolytica-induced cleavage of caspase-3, -6, and -7 were not inhibited by pretreatment of amoebae with wortmannin or staurosporin. In addition, we found that amoebic PI3K and PKC have an important role on amoeba adhesion to host compartment. These results suggest that amebic PI3K and PKC activation may play an important role in caspase-independent cell death in Entamoeba-induced apoptosis. The Korean Society for Parasitology and Tropical Medicine 2014-08 2014-08-29 /pmc/articles/PMC4170031/ /pubmed/25246714 http://dx.doi.org/10.3347/kjp.2014.52.4.355 Text en © 2014, Korean Society for Parasitology and Tropical Medicine http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Lee, Young Ah
Kim, Kyeong Ah
Min, Arim
Shin, Myeong Heon
spellingShingle Lee, Young Ah
Kim, Kyeong Ah
Min, Arim
Shin, Myeong Heon
Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica
author_facet Lee, Young Ah
Kim, Kyeong Ah
Min, Arim
Shin, Myeong Heon
author_sort Lee, Young Ah
title Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica
title_short Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica
title_full Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica
title_fullStr Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica
title_full_unstemmed Amoebic PI3K and PKC Is Required for Jurkat T Cell Death Induced by Entamoeba histolytica
title_sort amoebic pi3k and pkc is required for jurkat t cell death induced by entamoeba histolytica
description The enteric protozoan parasite Entamoeba histolytica is the causative agent of human amebiasis. During infection, adherence of E. histolytica through Gal/GalNAc lectin on the surface of the amoeba can induce caspase-3-dependent or -independent host cell death. Phosphorylinositol 3-kinase (PI3K) and protein kinase C (PKC) in E. histolytica play an important function in the adhesion, killing, or phagocytosis of target cells. In this study, we examined the role of amoebic PI3K and PKC in amoeba-induced apoptotic cell death in Jurkat T cells. When Jurkat T cells were incubated with E. histolytica trophozoites, phosphatidylserine (PS) externalization and DNA fragmentation in Jurkat cells were markedly increased compared to those of cells incubated with medium alone. However, when amoebae were pretreated with a PI3K inhibitor, wortmannin before being incubated with E. histolytica, E. histolytica-induced PS externalization and DNA fragmentation in Jurkat cells were significantly reduced compared to results for amoebae pretreated with DMSO. In addition, pretreatment of amoebae with a PKC inhibitor, staurosporine strongly inhibited Jurkat T cell death. However, E. histolytica-induced cleavage of caspase-3, -6, and -7 were not inhibited by pretreatment of amoebae with wortmannin or staurosporin. In addition, we found that amoebic PI3K and PKC have an important role on amoeba adhesion to host compartment. These results suggest that amebic PI3K and PKC activation may play an important role in caspase-independent cell death in Entamoeba-induced apoptosis.
publisher The Korean Society for Parasitology and Tropical Medicine
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4170031/
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