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Calpain‐dependent cleavage of SHP‐1 and SHP‐2 is involved in the dephosphorylation of Jurkat T cells induced by Entamoeba histolytica
Author(s) -
KIM K. A.,
LEE Y. A.,
SHIN M. H.
Publication year - 2010
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1111/j.1365-3024.2009.01175.x
Subject(s) - jurkat cells , dephosphorylation , entamoeba histolytica , biology , protein tyrosine phosphatase , microbiology and biotechnology , calpain , phosphorylation , tyrosine phosphorylation , programmed cell death , phosphatase , t cell , immune system , apoptosis , biochemistry , immunology , enzyme
Summary Host cell death induced by Entamoeba histolytica is an important mechanism for both host defence and microbial immune evasion during human amoebiasis. However, the signalling pathways underlying cell death induced by E. histolytica are not fully understood. This study investigated the involvement of the protein tyrosine phosphatases (PTPs) SHP‐1 and SHP‐2 in the dephosphorylation associated with E. histolytica ‐induced host cell death. Incubation with E. histolytica resulted in a marked decrease in protein tyrosine phosphorylation levels and degradation of SHP‐1 or SHP‐2 in Jurkat cells. Pre‐treatment of cells with a calpain inhibitor, calpeptin, impeded the amoeba‐induced dephosporylation and cleavage of SHP‐1 or SHP‐2. Additionally, inhibition of PTPs with phenylarsine oxide (PAO) attenuated Entamoeba ‐induced dephosphorylation and DNA fragmentation in Jurkat T cells. These results suggest that calpain‐dependent cleavage of SHP‐1 and SHP‐2 may contribute to protein tyrosine dephosphorylation in Jurkat T cell death induced by E. histolytica .