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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2008-3-14
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pubmed:abstractText |
Subtilase cytotoxin (SubAB) is a AB(5) type toxin produced by Shiga-toxigenic Escherichia coli, which exhibits cytotoxicity to Vero cells. SubAB B subunit binds to toxin receptors on the cell surface, whereas the A subunit is a subtilase-like serine protease that specifically cleaves chaperone BiP/Grp78. As noted previously, SubAB caused inhibition of protein synthesis. We now show that the inhibition of protein synthesis was transient and occurred as a result of ER stress induced by cleavage of BiP; it was closely associated with phosphorylation of double-stranded RNA-activated protein kinase-like ER kinase (PERK) and eukaryotic initiation factor-2alpha (eIF2alpha). The phosphorylation of PERK and eIF2alpha was maximal at 30-60 min and then returned to the control level. Protein synthesis after treatment of cells with SubAB was suppressed for 2 h and recovered, followed by induction of stress-inducible C/EBP-homologous protein (CHOP). BiP degradation continued, however, even after protein synthesis recovered. SubAB-treated cells showed cell cycle arrest in G1 phase, which may result from cyclin D1 downregulation caused by both SubAB-induced translational inhibition and continuous prolonged proteasomal degradation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-10411905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-11035797,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-11106749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-11381086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-12042763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-12370288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-14765132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-15226357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-15322075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-15543429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-15781103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-15814610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-1599691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-16176978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-16965518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-17024087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-17101670,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-3284526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-3298243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-3352747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-3571242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-7736585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-7758941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-7877684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-8513503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-8754828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-9136925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-9637683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-9665978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-9755171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-9819435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18005237-9930704
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1462-5822
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
921-9
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pubmed:dateRevised |
2011-7-20
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pubmed:meshHeading |
pubmed-meshheading:18005237-Animals,
pubmed-meshheading:18005237-Blotting, Western,
pubmed-meshheading:18005237-Cell Cycle,
pubmed-meshheading:18005237-Cercopithecus aethiops,
pubmed-meshheading:18005237-Cyclin D1,
pubmed-meshheading:18005237-Escherichia coli Proteins,
pubmed-meshheading:18005237-Flow Cytometry,
pubmed-meshheading:18005237-G1 Phase,
pubmed-meshheading:18005237-Heat-Shock Proteins,
pubmed-meshheading:18005237-Molecular Chaperones,
pubmed-meshheading:18005237-Protein Biosynthesis,
pubmed-meshheading:18005237-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:18005237-Shiga-Toxigenic Escherichia coli,
pubmed-meshheading:18005237-Subtilisins,
pubmed-meshheading:18005237-Vero Cells
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pubmed:year |
2008
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pubmed:articleTitle |
Subtilase cytotoxin, produced by Shiga-toxigenic Escherichia coli, transiently inhibits protein synthesis of Vero cells via degradation of BiP and induces cell cycle arrest at G1 by downregulation of cyclin D1.
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pubmed:affiliation |
Department of Molecular Infectiology, Graduate School of Medicine, Chiba University, 1-8- Inohana,Chiba 260-8670, Japan. nmorinaga@faculty.chiba-u.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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