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EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival

Mitogen Activated Protein Kinases (MAPKs) are a class of serine/threonine kinases that regulate a number of different cellular activities including cell proliferation, differentiation, survival and even death. The pathogen Entamoeba histolytica possess a single homologue of a typical MAPK gene (EhMA...

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Published in:PloS one 2010-10, Vol.5 (10), p.e13291
Main Authors: Ghosh, Anupama Sardar, Ray, Doel, Dutta, Suman, Raha, Sanghamitra
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description Mitogen Activated Protein Kinases (MAPKs) are a class of serine/threonine kinases that regulate a number of different cellular activities including cell proliferation, differentiation, survival and even death. The pathogen Entamoeba histolytica possess a single homologue of a typical MAPK gene (EhMAPK) whose identification was previously reported by us but its functional implications remained unexplored. EhMAPK, the only mitogen-activated protein kinase from the parasitic protist Entamoeba histolytica with Threonine-X-Tyrosine (TXY) phosphorylation motif was cloned, expressed in E. coli and functionally characterized under different stress conditions. The expression profile of EhMAPK at the protein and mRNA level remained similar among untreated, heat shocked and hydrogen peroxide-treated samples in all cases of dose and time. But a significant difference was obtained in the phosphorylation status of the protein in response to different stresses. Heat shock at 43°C or 0.5 mM H(2)O(2) treatment enhanced the phosphorylation status of EhMAPK and augmented the kinase activity of the protein whereas 2.0 mM H(2)O(2) treatment induced dephosphorylation of EhMAPK and loss of kinase activity. 2.0 mM H(2)O(2) treatment reduced parasite viability significantly but heat shock and 0.5 mM H(2)O(2) treatment failed to adversely affect E. histolytica viability. Therefore, a distinct possibility that activation of EhMAPK is associated with stress survival in E. histolytica is seen. Our study also gives a glimpse of the regulatory mechanism of the protein under in vivo conditions. Since the parasite genome lacks any typical homologue of mammalian MEK, the dual specificity kinases which are the upstream activators of MAPK, indications of the existence of some alternate regulatory mechanisms of the EhMAPK activity is perceived. These may include the autophosphorylation activity of the protein itself in combination with some upstream phosphatases which are not yet identified.
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Gordon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2010-10-08</date><risdate>2010</risdate><volume>5</volume><issue>10</issue><spage>e13291</spage><pages>e13291-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Mitogen Activated Protein Kinases (MAPKs) are a class of serine/threonine kinases that regulate a number of different cellular activities including cell proliferation, differentiation, survival and even death. The pathogen Entamoeba histolytica possess a single homologue of a typical MAPK gene (EhMAPK) whose identification was previously reported by us but its functional implications remained unexplored. EhMAPK, the only mitogen-activated protein kinase from the parasitic protist Entamoeba histolytica with Threonine-X-Tyrosine (TXY) phosphorylation motif was cloned, expressed in E. coli and functionally characterized under different stress conditions. The expression profile of EhMAPK at the protein and mRNA level remained similar among untreated, heat shocked and hydrogen peroxide-treated samples in all cases of dose and time. But a significant difference was obtained in the phosphorylation status of the protein in response to different stresses. Heat shock at 43°C or 0.5 mM H(2)O(2) treatment enhanced the phosphorylation status of EhMAPK and augmented the kinase activity of the protein whereas 2.0 mM H(2)O(2) treatment induced dephosphorylation of EhMAPK and loss of kinase activity. 2.0 mM H(2)O(2) treatment reduced parasite viability significantly but heat shock and 0.5 mM H(2)O(2) treatment failed to adversely affect E. histolytica viability. Therefore, a distinct possibility that activation of EhMAPK is associated with stress survival in E. histolytica is seen. Our study also gives a glimpse of the regulatory mechanism of the protein under in vivo conditions. Since the parasite genome lacks any typical homologue of mammalian MEK, the dual specificity kinases which are the upstream activators of MAPK, indications of the existence of some alternate regulatory mechanisms of the EhMAPK activity is perceived. These may include the autophosphorylation activity of the protein itself in combination with some upstream phosphatases which are not yet identified.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>20949043</pmid><doi>10.1371/journal.pone.0013291</doi><tpages>e13291</tpages><oa>free_for_read</oa></addata></record>
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subjects Amino Acid Sequence
Animals
Base Sequence
Biochemistry/Cell Signaling and Trafficking Structures
Blotting, Western
Cell Biology/Cell Signaling
Cell Biology/Cellular Death and Stress Responses
Cell growth
Cell proliferation
Cell Survival
Cloning
Crystallography
Cytokines
Deoxyribonucleic acid
Dephosphorylation
DNA
DNA damage
DNA Primers
E coli
Entamoeba histolytica
Entamoeba histolytica - enzymology
Epidermal growth factor
Gene expression
Genomes
Genomics
Heat shock
Homology
Hydrogen
Hydrogen peroxide
Hydrogen Peroxide - pharmacology
Immunoprecipitation
Infectious Diseases/Neglected Tropical Diseases
Kinases
Leukemia
Mammals
MAP kinase
Mitogen-Activated Protein Kinases - chemistry
Mitogen-Activated Protein Kinases - metabolism
Mitogens
Molecular biology
Molecular Sequence Data
mRNA
Mutagenesis, Site-Directed
Nuclear physics
Oxidative stress
Parasites
Parasitic diseases
Phosphatase
Phosphatases
Phosphorylation
Plasmodium falciparum
Protein kinase
Protein kinases
Proteins
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Regulatory mechanisms (biology)
Reverse Transcriptase Polymerase Chain Reaction
RNA
Rodents
Sequence Homology, Amino Acid
Serine
Signal transduction
Survival
Threonine
Tyrosine
Viability
title EhMAPK, the mitogen-activated protein kinase from Entamoeba histolytica is associated with cell survival
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