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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
2007-8-28
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pubmed:abstractText |
Mono ADP-ribosyltransferases (ARTs) are a family of enzymes related to bacterial toxins that possess adenosine diphosphate ribosyltransferase activity. We have assessed that A549 constitutively expressed ART1 on the cell surface and shown that lipotheicoic acid (LTA) and flagellin, but not lipopolysaccharide (LPS), peptidoglycan (PG) and poly (I:C), up-regulate ART1 in a time and dose dependent manner. These agonists did not alter the expression of ART3 and ART5 genes. Indeed, LTA and flagellin stimulation increased the level of ART1 protein and transcript while ART4 gene was activated after stimulation of cells with LPS, LTA, PAM and PG via TLR2 and TLR4 receptors. These results show that human ARTs possess a differential capacity to respond to bacteria cell wall components and might play a crucial role in innate immune response in airways.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Flagellin,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Pam(3)CSK(4) peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidoglycan,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Teichoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/lipoteichoic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4199-204
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17707376-ADP Ribose Transferases,
pubmed-meshheading:17707376-Animals,
pubmed-meshheading:17707376-Arginine,
pubmed-meshheading:17707376-Bacterial Toxins,
pubmed-meshheading:17707376-Cell Line,
pubmed-meshheading:17707376-Cricetinae,
pubmed-meshheading:17707376-Cricetulus,
pubmed-meshheading:17707376-Enzyme Activation,
pubmed-meshheading:17707376-Epithelial Cells,
pubmed-meshheading:17707376-Flagellin,
pubmed-meshheading:17707376-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:17707376-Humans,
pubmed-meshheading:17707376-Lipopeptides,
pubmed-meshheading:17707376-Lipopolysaccharides,
pubmed-meshheading:17707376-Peptides,
pubmed-meshheading:17707376-Peptidoglycan,
pubmed-meshheading:17707376-Pulmonary Alveoli,
pubmed-meshheading:17707376-RNA, Messenger,
pubmed-meshheading:17707376-Substrate Specificity,
pubmed-meshheading:17707376-Teichoic Acids,
pubmed-meshheading:17707376-Up-Regulation
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pubmed:year |
2007
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pubmed:articleTitle |
Expression and selective up-regulation of toxin-related mono ADP-ribosyltransferases by pathogen-associated molecular patterns in alveolar epithelial cells.
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pubmed:affiliation |
Department of Comparative Morphology and Biochemistry, University of Camerino, 62032 Camerino, Italy. enrico_balducci@chiron.com
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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