Calpain-dependent cleavage of SHP-1 and SHP-2 is involved in the dephosphorylation of Jurkat T cells induced by Entamoeba histolytica

Parasite Immunology

Volumn 32, Issue 3, 2010, Pages 176-183

  Kim, K A ^a   Lee, Y A ^a   Shin, M H ^a  

^a Yonsei University College of Medicine   (South Korea)

Author keywords

Calpain; Cell death; Dephosphorylation; Entamoeba histolytica; Host cell; Tyrosine phosphatase SHP 1 and SHP 2

Indexed keywords

ARSENOSOBENZENE; CALPAIN; CALPEPTIN; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEIN TYROSINE PHOSPHATASE SHP 2;

ARTICLE; CELL DEATH; DNA FRAGMENTATION; ENTAMOEBA HISTOLYTICA; HOST CELL; HUMAN; HUMAN CELL; INCUBATION TIME; LEUKEMIA CELL LINE; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEPHOSPHORYLATION; T LYMPHOCYTE;

ARSENICALS; CALPAIN; CELL DEATH; DIPEPTIDES; ENTAMOEBA HISTOLYTICA; ENZYME INHIBITORS; HUMANS; JURKAT CELLS; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 11; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 6; T-LYMPHOCYTES;

ENTAMOEBA; ENTAMOEBA HISTOLYTICA;

EID: 76749171760     PISSN: 01419838     EISSN: 13653024     Source Type: Journal    
DOI: 10.1111/j.1365-3024.2009.01175.x     Document Type: Article

References (28)

1. Huston CD. Parasite and host contributions to the pathogenesis of amebic colitis. Trend Parasitol 2004 20 : 23 26.
2. Kim JM, Jung HC, Im K, Cho YJ Kim CY. Interleukin-8 gene expression in the human colon epithelial cell line, HT-29, exposed to Entamoeba histolytica. Korean J Parasitol 1995 33 : 357 364.
3. Seydel KB, Li E, Zhang Z Stanley SL Jr. Epithelial cell-initiated inflammation plays a crucial role in early tissue damage in amebic infection of human intestine. Gastroenterology 1998 115 : 1446 1453.
4. Petri WA Jr., Haque R Mann BJ. The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica. Annu Rev Microbiol 2002 56 : 39 64.
5. 2-integrin in ROS-mediated neutrophil apoptosis induced by Entamoeba histolytica. Microb Infect 2007 9 : 1368 1375.
6. Huston CD, Houpt ER, Mann BJ, Hahn CS Petri WA Jr. Caspase 3-dependent killing of host cells by the parasite Entamoeba histolytica. Cell Microbiol 2000 2 : 617 625.
7. Ravdin JI, Sperelakis N Guerrant RL. Effect of ion channel inhibitors on the cytopathogenicity of Entamoeba histolytica. J Infect Dis 1982 146 : 335 340.
8. Kim KA, Lee YA Shin MH. Calpain-dependent calpastatin cleavage regulates caspase-3 activation during apoptosis of Jurkat T cells induced by Entamoeba histolytica. Int J Parasitol 2007 37 : 1209 1219.
9. Sim S, Yong TS, Park SJ, et al. NADPH oxidase-derived reactive oxygen species-mediated activation of ERK1/2 is required for apoptosis of human neutrophils induced by Entamoeba histolytica. J Immunol 2005 174 : 4279 4288.
10. Martiny A, Meyer-Fernandes JR, de Souza W Vannier-Santos MA. Altered tyrosine phosphorylation of ERK1/2 MAP kinase and other macrophage molecules caused by Leishmania amastigotes. Mol Biochem Parasitol 1999 102 : 1 12.
11. Chong ZZ Maiese K. The Src homology 2 domain tyrosine phosphatases SHP-1 and SHP-2: diversified control of cell growth, inflammation, and injury. Histol Histopathol 2007 22 : 1251 1267.
12. Neel BG, Gu H Pao L. The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trend Biochem Sci 2003 28 : 284 293.
13. Wang N, Li Z, Ding R, et al. Antagonism or synergism. Role of tyrosine phosphatases SHP-1 and SHP-2 in growth factor signaling. J Biol Chem 2006 281 : 21878 21883.
14. Haque SJ, Harbor P, Tabrizi M, Yi T Williams BR. Protein-tyrosine phosphatase Shp-1 is a negative regulator of IL-4 and IL-13-dependent signal transduction. J Biol Chem 1998 18 : 33893 33896.
15. Ram PA Waxman DJ. Interaction of growth hormone-activated STATs with SH2-containing phosphotyrosine phosphatase SHP-1 and nuclear JAK2 tyrosine kinase. J Biol Chem 1997 272 : 17694 17702.
16. Kui QC. The SHP-2 tyrosine phosphatase: signaling mechanisms and biological functions. Cell Res 2000 10 : 279 288.
17. Chen J, Yu WM, Bunting KD Qu CK. A negative role of SHP-2 tyrosine phosphatase in growth factor-dependent hematopoietic cell survival. Oncogene 2004 23 : 3659 3669.
18. Falet H, Pain S Rendu F. Tyrosine unphosphorylated platelet SHP-1 is a substrate for calpain. Biochem Biophys Res Commun 1998 252 : 51 56.
19. Gu M Majerus PW. The properties of the protein tyrosine phosphatases PTPMEG. J Biol Chem 1996 127 : 27751 27759.
20. Pasquet JM, Dachary-Prigent J Nurden AT. Microvesicle release is associated with extensive protein tyrosine dephosphorylation in platelets stimulated by A23187 or a mixture of thrombin and collagen. Biochem J 1998 333 : 591 599.
21. Teixeira JE Mann BJ. Entamoeba histolytica-induced dephosphorylation in host cells. Infect Immun 2002 70 : 1816 1823.
22. Lu W, Gong D, Bar-Sagi D Cole PA. Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling. Mol Cell 2001 8 : 759 769.
23. Zhang Z, Shen K, Lu W Cole PA. The role of C-terminal tyrosine phosphorylation in the regulation of SHP-1 explored via expressed protein ligation. J Biol Chem 2003 278 : 4668 4674.
24. Chen K, Thomas SR Keaney JF Jr. Beyond LDL oxidation: ROS in vascular signal transduction. Free Radic Biol Med 2003 35 : 117 132.
25. Pei D, Lorenz U, Klingmuller U, Neel BG Walsh CT. Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains. Biochemistry 1994 33 : 15483 15493.
26. Schoenwaelder SM, Kulkarni S, Salem HH, et al. Distinct substrate specificities and functional roles for the 78- and 76-kDa forms of μ-calpain in human platelets. J Biol Chem 1997 272 : 24876 24884.
27. Knutson KL, Hmama Z, Herrera-Velit P, Rochford R Reiner NE. Lipoarabinomannan of Mycobacterium tuberculosis promotes protein tyrosine dephosphorylation and inhibition of mitogen-activated protein kinase in human mononuclear phagocytes. Role of the Src homology 2 containing tyrosine phosphatase 1. J Biol Chem 1998 273 : 645 652.
28. Tsutsumi R, Takahashi A, Azuma T, Higashi H Hatakeyama M. Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA. Mol Cell Biol 2006 26 : 261 276.