Source:http://linkedlifedata.com/resource/pubmed/id/10361307
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1999-9-15
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pubmed:abstractText |
The exoenzyme S (ExoS)-producing Pseudomonas aeruginosa strain, 388, and corresponding ExoS knock-out strain, 388deltaexoS, were used in a bacterial and mammalian co-culture system as a model for the contact-dependent delivery of ExoS into host cells. Examination of DNA synthesis and Ras ADP-ribosylation in tumour cell lines expressing normal and mutant Ras revealed a decrease in DNA synthesis concomitant with ADP-ribosylation of Ras proteins after exposure to ExoS-producing bacteria, but not after exposure to non-ExoS-producing bacteria. Examination of normal H-Ras, K-Ras and N-Ras by two-dimensional electrophoresis after exposure to bacteria revealed differences in the degree of ADP-ribosylation by ExoS, with H-Ras being modified most extensively. ADP-ribosylation of oncogenic forms of Ras was examined in vivo using cancer lines expressing mutant forms of H-, N- or K-Ras. The mutant Ras proteins were modified in a manner qualitatively similar to their normal counterparts. Using Ras/Raf-1 co-immunoprecipitation after co-culture, it was found that exposure to ExoS-producing bacteria caused a decrease in the amount of Raf-1 associated with EGF-activated Ras and oncogenic Ras. The results from this study indicate that ExoS ADP-ribosylates both normal and mutant Ras proteins in vivo and inhibits signalling through Ras.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-raf,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/exoenzyme S,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1054-64
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10361307-ADP Ribose Transferases,
pubmed-meshheading:10361307-Adenosine Diphosphate Ribose,
pubmed-meshheading:10361307-Bacterial Toxins,
pubmed-meshheading:10361307-Blotting, Western,
pubmed-meshheading:10361307-Cell Line,
pubmed-meshheading:10361307-Coculture Techniques,
pubmed-meshheading:10361307-DNA,
pubmed-meshheading:10361307-Densitometry,
pubmed-meshheading:10361307-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:10361307-Precipitin Tests,
pubmed-meshheading:10361307-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:10361307-Pseudomonas aeruginosa,
pubmed-meshheading:10361307-Recombinant Proteins,
pubmed-meshheading:10361307-Tumor Cells, Cultured,
pubmed-meshheading:10361307-ras Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
ADP-ribosylation of oncogenic Ras proteins by pseudomonas aeruginosa exoenzyme S in vivo.
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pubmed:affiliation |
Departments of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston 29425, USA. vincents@musc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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