Calyculin A sensitive protein phosphatase is required for Bacillus anthracis lethal toxin induced cytotoxicity
Previous studies have shown that the Bacillus anthracis lethal toxin can induce both necrosis and apoptosis in mouse macrophage-like J774A.1 cells depending on both the toxin concentration and the phosphatase activity. In this study several protein kinase or phosphatase inhibitors were employed to e...
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| Veröffentlicht in: | Current microbiology 2002-02, Vol.44 (2), p.106-111 |
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| creator | KAU, Jyh-Hwa LIN, Ching-Gong HUANG, Hsin-Hsien HSU, Hui-Ling CHEN, Kuo-Ching WU, Yu-Ping LIN, Hung-Chi |
| description | Previous studies have shown that the Bacillus anthracis lethal toxin can induce both necrosis and apoptosis in mouse macrophage-like J774A.1 cells depending on both the toxin concentration and the phosphatase activity. In this study several protein kinase or phosphatase inhibitors were employed to evaluate the hypothesis that the lethal toxin induces cell death via protein phosphorylation processes. Pretreatment with a serine/threonine phosphatase inhibitor Calyculin A (300 nM) could inhibit about 78% of cell death induced by the lethal toxin, whereas inhibitors of kinases, such as H7, HA, Sphingosine, and Genestein, but other inhibitors of phosphatases, such as Okadaic acid, Tautomycin, and Cyclosporin A, did not. In addition, recent reports have demonstrated that the MEK1 protein may serve as a proteolytic target within its N-terminus for lethal factor cleavage. In this study, Calyculin A is shown to enhance the phosphorylation of the MEK1 protein. This prevents the cleavage of the MEK1 by lethal factor. These results suggest that a putative Calyculin A-sensitive protein phosphatase is involved in anthrax toxin induced cytotoxicity and that the blocking effect of Calyculin A on lethal factor cytotoxicity may be mediated through the MEK signaling pathway. |
| doi_str_mv | 10.1007/s00284-001-0059-8 |
| format | Article |
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In this study several protein kinase or phosphatase inhibitors were employed to evaluate the hypothesis that the lethal toxin induces cell death via protein phosphorylation processes. Pretreatment with a serine/threonine phosphatase inhibitor Calyculin A (300 nM) could inhibit about 78% of cell death induced by the lethal toxin, whereas inhibitors of kinases, such as H7, HA, Sphingosine, and Genestein, but other inhibitors of phosphatases, such as Okadaic acid, Tautomycin, and Cyclosporin A, did not. In addition, recent reports have demonstrated that the MEK1 protein may serve as a proteolytic target within its N-terminus for lethal factor cleavage. In this study, Calyculin A is shown to enhance the phosphorylation of the MEK1 protein. This prevents the cleavage of the MEK1 by lethal factor. These results suggest that a putative Calyculin A-sensitive protein phosphatase is involved in anthrax toxin induced cytotoxicity and that the blocking effect of Calyculin A on lethal factor cytotoxicity may be mediated through the MEK signaling pathway.</description><identifier>ISSN: 0343-8651</identifier><identifier>EISSN: 1432-0991</identifier><identifier>DOI: 10.1007/s00284-001-0059-8</identifier><identifier>PMID: 11815854</identifier><identifier>CODEN: CUMIDD</identifier><language>eng</language><publisher>New York, NY: Springer</publisher><subject>Animals ; Anthrax ; Antifungal Agents - pharmacology ; Antigens, Bacterial ; Apoptosis ; Bacillus anthracis ; Bacillus anthracis - enzymology ; Bacillus anthracis - metabolism ; Bacillus anthracis - pathogenicity ; Bacterial diseases ; Bacterial sepsis ; Bacterial Toxins - metabolism ; Bacterial Toxins - toxicity ; Bacteriology ; Biological and medical sciences ; Blotting, Western ; Cells, Cultured ; Cyclosporine - pharmacology ; Cytotoxicity ; Enzyme Inhibitors - pharmacology ; Fundamental and applied biological sciences. Psychology ; Genistein - pharmacology ; Human bacterial diseases ; Infectious diseases ; Inhibitors ; Kinases ; MAP Kinase Kinase Kinase 1 ; Medical sciences ; MEK1 protein ; Metabolism. Enzymes ; Mice ; Microbiology ; Okadaic Acid - pharmacology ; Oxazoles - pharmacology ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Phosphoprotein Phosphatases - metabolism ; Phosphorylation ; protein phosphatase ; Protein-Serine-Threonine Kinases - antagonists & inhibitors ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; Pyrans ; Signal Transduction - drug effects ; Sphingosine - pharmacology ; Spiro Compounds ; Toxins</subject><ispartof>Current microbiology, 2002-02, Vol.44 (2), p.106-111</ispartof><rights>Springer-Verlag New York Inc. 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-654fea48c03e3bbe98cecb3f208513456723655b0c47f19c36a3b3b84365096e3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,27929,27930</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14245030$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11815854$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KAU, Jyh-Hwa</creatorcontrib><creatorcontrib>LIN, Ching-Gong</creatorcontrib><creatorcontrib>HUANG, Hsin-Hsien</creatorcontrib><creatorcontrib>HSU, Hui-Ling</creatorcontrib><creatorcontrib>CHEN, Kuo-Ching</creatorcontrib><creatorcontrib>WU, Yu-Ping</creatorcontrib><creatorcontrib>LIN, Hung-Chi</creatorcontrib><title>Calyculin A sensitive protein phosphatase is required for Bacillus anthracis lethal toxin induced cytotoxicity</title><title>Current microbiology</title><addtitle>Curr Microbiol</addtitle><description>Previous studies have shown that the Bacillus anthracis lethal toxin can induce both necrosis and apoptosis in mouse macrophage-like J774A.1 cells depending on both the toxin concentration and the phosphatase activity. In this study several protein kinase or phosphatase inhibitors were employed to evaluate the hypothesis that the lethal toxin induces cell death via protein phosphorylation processes. Pretreatment with a serine/threonine phosphatase inhibitor Calyculin A (300 nM) could inhibit about 78% of cell death induced by the lethal toxin, whereas inhibitors of kinases, such as H7, HA, Sphingosine, and Genestein, but other inhibitors of phosphatases, such as Okadaic acid, Tautomycin, and Cyclosporin A, did not. In addition, recent reports have demonstrated that the MEK1 protein may serve as a proteolytic target within its N-terminus for lethal factor cleavage. In this study, Calyculin A is shown to enhance the phosphorylation of the MEK1 protein. This prevents the cleavage of the MEK1 by lethal factor. These results suggest that a putative Calyculin A-sensitive protein phosphatase is involved in anthrax toxin induced cytotoxicity and that the blocking effect of Calyculin A on lethal factor cytotoxicity may be mediated through the MEK signaling pathway.</description><subject>Animals</subject><subject>Anthrax</subject><subject>Antifungal Agents - pharmacology</subject><subject>Antigens, Bacterial</subject><subject>Apoptosis</subject><subject>Bacillus anthracis</subject><subject>Bacillus anthracis - enzymology</subject><subject>Bacillus anthracis - metabolism</subject><subject>Bacillus anthracis - pathogenicity</subject><subject>Bacterial diseases</subject><subject>Bacterial sepsis</subject><subject>Bacterial Toxins - metabolism</subject><subject>Bacterial Toxins - toxicity</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cells, Cultured</subject><subject>Cyclosporine - pharmacology</subject><subject>Cytotoxicity</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genistein - pharmacology</subject><subject>Human bacterial diseases</subject><subject>Infectious diseases</subject><subject>Inhibitors</subject><subject>Kinases</subject><subject>MAP Kinase Kinase Kinase 1</subject><subject>Medical sciences</subject><subject>MEK1 protein</subject><subject>Metabolism. Enzymes</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Okadaic Acid - pharmacology</subject><subject>Oxazoles - pharmacology</subject><subject>Phosphoprotein Phosphatases - antagonists & inhibitors</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylation</subject><subject>protein phosphatase</subject><subject>Protein-Serine-Threonine Kinases - antagonists & inhibitors</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proteins</subject><subject>Pyrans</subject><subject>Signal Transduction - drug effects</subject><subject>Sphingosine - pharmacology</subject><subject>Spiro Compounds</subject><subject>Toxins</subject><issn>0343-8651</issn><issn>1432-0991</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp90U1rGzEQBmARWhLH7Q_IJQhKSy7bavSxKx1T0ySFQC_tWWjlWawg7zqSNsT_vjI2BHroQQgNzwyMXkKugH0FxrpvmTGuZcMY1KNMo8_IAqTgDTMG3pEFE1I0ulVwQS5zfqqOGwbn5AJAg9JKLsi4cnHv5xhGekszjjmU8IJ0l6aCtbbbTHm3ccVlpCHThM9zSLimw5Tod-dDjHOmbiybVB-ZRiwbF2mZXmtvGNezr9bvy3So-FD2H8j7wcWMH0_3kvy5-_F79dA8_rr_ubp9bLwCWZpWyQGd1J4JFH2PRnv0vRg40wqEVG3HRatUz7zsBjBetE70oteyVplpUSzJl-PcusjzjLnYbcgeY3QjTnO2oHnLBecV3vwfSqk5h86ISj_9Q5-mOY11jaoEmK41lS0JHJVPU84JB7tLYevS3gKzh9TsMTVb07CH1KyuPdenyXO_xfVbxymmCj6fgMvexSG5sX73m5NcKiaY-AseNZ-S</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>KAU, Jyh-Hwa</creator><creator>LIN, Ching-Gong</creator><creator>HUANG, Hsin-Hsien</creator><creator>HSU, Hui-Ling</creator><creator>CHEN, Kuo-Ching</creator><creator>WU, Yu-Ping</creator><creator>LIN, Hung-Chi</creator><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7U7</scope></search><sort><creationdate>20020201</creationdate><title>Calyculin A sensitive protein phosphatase is required for Bacillus anthracis lethal toxin induced cytotoxicity</title><author>KAU, Jyh-Hwa ; LIN, Ching-Gong ; HUANG, Hsin-Hsien ; HSU, Hui-Ling ; CHEN, Kuo-Ching ; WU, Yu-Ping ; LIN, Hung-Chi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-654fea48c03e3bbe98cecb3f208513456723655b0c47f19c36a3b3b84365096e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Anthrax</topic><topic>Antifungal Agents - pharmacology</topic><topic>Antigens, Bacterial</topic><topic>Apoptosis</topic><topic>Bacillus anthracis</topic><topic>Bacillus anthracis - enzymology</topic><topic>Bacillus anthracis - metabolism</topic><topic>Bacillus anthracis - pathogenicity</topic><topic>Bacterial diseases</topic><topic>Bacterial sepsis</topic><topic>Bacterial Toxins - metabolism</topic><topic>Bacterial Toxins - toxicity</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cells, Cultured</topic><topic>Cyclosporine - pharmacology</topic><topic>Cytotoxicity</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genistein - pharmacology</topic><topic>Human bacterial diseases</topic><topic>Infectious diseases</topic><topic>Inhibitors</topic><topic>Kinases</topic><topic>MAP Kinase Kinase Kinase 1</topic><topic>Medical sciences</topic><topic>MEK1 protein</topic><topic>Metabolism. Enzymes</topic><topic>Mice</topic><topic>Microbiology</topic><topic>Okadaic Acid - pharmacology</topic><topic>Oxazoles - pharmacology</topic><topic>Phosphoprotein Phosphatases - antagonists & inhibitors</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>protein phosphatase</topic><topic>Protein-Serine-Threonine Kinases - antagonists & inhibitors</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proteins</topic><topic>Pyrans</topic><topic>Signal Transduction - drug effects</topic><topic>Sphingosine - pharmacology</topic><topic>Spiro Compounds</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KAU, Jyh-Hwa</creatorcontrib><creatorcontrib>LIN, Ching-Gong</creatorcontrib><creatorcontrib>HUANG, Hsin-Hsien</creatorcontrib><creatorcontrib>HSU, Hui-Ling</creatorcontrib><creatorcontrib>CHEN, Kuo-Ching</creatorcontrib><creatorcontrib>WU, 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Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Toxicology Abstracts</collection><jtitle>Current microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KAU, Jyh-Hwa</au><au>LIN, Ching-Gong</au><au>HUANG, Hsin-Hsien</au><au>HSU, Hui-Ling</au><au>CHEN, Kuo-Ching</au><au>WU, Yu-Ping</au><au>LIN, Hung-Chi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Calyculin A sensitive protein phosphatase is required for Bacillus anthracis lethal toxin induced cytotoxicity</atitle><jtitle>Current microbiology</jtitle><addtitle>Curr Microbiol</addtitle><date>2002-02-01</date><risdate>2002</risdate><volume>44</volume><issue>2</issue><spage>106</spage><epage>111</epage><pages>106-111</pages><issn>0343-8651</issn><eissn>1432-0991</eissn><coden>CUMIDD</coden><abstract>Previous studies have shown that the Bacillus anthracis lethal toxin can induce both necrosis and apoptosis in mouse macrophage-like J774A.1 cells depending on both the toxin concentration and the phosphatase activity. In this study several protein kinase or phosphatase inhibitors were employed to evaluate the hypothesis that the lethal toxin induces cell death via protein phosphorylation processes. Pretreatment with a serine/threonine phosphatase inhibitor Calyculin A (300 nM) could inhibit about 78% of cell death induced by the lethal toxin, whereas inhibitors of kinases, such as H7, HA, Sphingosine, and Genestein, but other inhibitors of phosphatases, such as Okadaic acid, Tautomycin, and Cyclosporin A, did not. In addition, recent reports have demonstrated that the MEK1 protein may serve as a proteolytic target within its N-terminus for lethal factor cleavage. In this study, Calyculin A is shown to enhance the phosphorylation of the MEK1 protein. This prevents the cleavage of the MEK1 by lethal factor. These results suggest that a putative Calyculin A-sensitive protein phosphatase is involved in anthrax toxin induced cytotoxicity and that the blocking effect of Calyculin A on lethal factor cytotoxicity may be mediated through the MEK signaling pathway.</abstract><cop>New York, NY</cop><pub>Springer</pub><pmid>11815854</pmid><doi>10.1007/s00284-001-0059-8</doi><tpages>6</tpages></addata></record> |
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| ispartof | Current microbiology, 2002-02, Vol.44 (2), p.106-111 |
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| subjects | Animals Anthrax Antifungal Agents - pharmacology Antigens, Bacterial Apoptosis Bacillus anthracis Bacillus anthracis - enzymology Bacillus anthracis - metabolism Bacillus anthracis - pathogenicity Bacterial diseases Bacterial sepsis Bacterial Toxins - metabolism Bacterial Toxins - toxicity Bacteriology Biological and medical sciences Blotting, Western Cells, Cultured Cyclosporine - pharmacology Cytotoxicity Enzyme Inhibitors - pharmacology Fundamental and applied biological sciences. Psychology Genistein - pharmacology Human bacterial diseases Infectious diseases Inhibitors Kinases MAP Kinase Kinase Kinase 1 Medical sciences MEK1 protein Metabolism. Enzymes Mice Microbiology Okadaic Acid - pharmacology Oxazoles - pharmacology Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - metabolism Phosphorylation protein phosphatase Protein-Serine-Threonine Kinases - antagonists & inhibitors Protein-Serine-Threonine Kinases - metabolism Proteins Pyrans Signal Transduction - drug effects Sphingosine - pharmacology Spiro Compounds Toxins |
| title | Calyculin A sensitive protein phosphatase is required for Bacillus anthracis lethal toxin induced cytotoxicity |
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