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Calpain-dependent calpastatin cleavage regulates caspase-3 activation during apoptosis of Jurkat T cells induced by Entamoeba histolytica

Authors
 Kyeong Ah Kim  ;  Young Ah Lee  ;  Myeong Heon Shin 
Citation
 INTERNATIONAL JOURNAL FOR PARASITOLOGY, Vol.37(11) : 1209-1219, 2007 
Journal Title
 INTERNATIONAL JOURNAL FOR PARASITOLOGY 
ISSN
 0020-7519 
Issue Date
2007
MeSH
Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Apoptosis ; Calcium/metabolism ; Calcium-Binding Proteins/genetics* ; Calpain/metabolism ; Caspase 3/metabolism* ; Caspase Inhibitors ; DNA Cleavage* ; Dipeptides/pharmacology ; Entamoeba histolytica/metabolism* ; Entamoebiasis/enzymology* ; Entamoebiasis/immunology ; Entamoebiasis/pathology ; Enzyme Activation ; Host-Parasite Interactions ; Humans ; Jurkat Cells ; Parasitology/methods ; T-Lymphocytes/enzymology* ; T-Lymphocytes/pathology
Abstract
In this study, we investigated whether there is a signalling interaction between calpain and caspase-3 during apoptosis in Jurkat T cells by Entamoeba histolytica. When Jurkat cells were co-incubated with E. histolytica, phosphatidylserine externalisation and DNA fragmentation markedly increased compared with results for cells incubated with medium alone. In addition, E. histolytica strongly induced cleavage of caspases-3, -6, -7 and poly(ADP-ribose) polymerase. A rise in intracellular calcium levels and activation of calpain were seen in Jurkat cells after exposure to E. histolytica. Pretreatment of Jurkat cells with calpain inhibitor calpeptin effectively blocked E. histolytica-triggered cleavage of caspase-3 as well as calpain. In contrast, pan-caspase inhibitor did not affect E. histolytica-induced calpain activation. In addition, incubation with E. histolytica resulted in multiple fragmented bands of calpastatin, which is an endogenous inhibitor of calpain, in Jurkat T cells. Moreover, Entamoeba-induced calpastatin degradation was dramatically suppressed by pretreatment with calpeptin, but not by z-VAD-fmk. Entamoeba-induced DNA fragmentation was strongly retarded by z-VAD-fmk, but not calpeptin. Our results suggest that calpain-mediated calpastatin degradation plays a crucial role in regulation of caspase-3 activation during apoptosis of Jurkat T cells by E. histolytica.
Full Text
http://www.sciencedirect.com/science/article/pii/S0020751907001063
DOI
10.1016/j.ijpara.2007.03.011
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Kyung Ah(김경아)
Shin, Myeong Heon(신명헌) ORCID logo https://orcid.org/0000-0001-8207-6110
Lee, Young Ah(이영아) ORCID logo https://orcid.org/0000-0002-0414-842X
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/96127
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