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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1993-8-26
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pubmed:abstractText |
The conditioned medium of the murine macrophage PU5.1.8 was analyzed by two-dimensional gel electrophoresis in order to detect LPS-induced proteins. Spots of interest were identified by microsequencing of internal peptides generated by limited in situ acid hydrolysis. In total conditioned medium, several monokines (TNF-alpha and macrophage inflammatory protein-1 alpha and 1 beta) were identified as LPS-induced spots. Because minor spots could be masked by the complexity of the 2-D pattern, conditioned medium was successively fractionated by zinc precipitation and affinity chromatography (Procion red and Con A agarose). Zinc supernatant fraction, Procion red flow-through, and Con A eluate fractions were further analyzed by 2-D gel electrophoresis for the presence of LPS-induced spots. In these fractions serum amyloid A3, lipocalin 24p3, cathepsin B, and plasminogen activator inhibitor-I were characterized as LPS-induced proteins secreted by macrophages. Lipocalin 24p3 protein was retrieved for the first time. In addition to these proteins that follow a classical secretory pathway, several cellular proteins (mainly ribosomal proteins) were retrieved as LPS-induced proteins in the conditioned medium. Control experiments argue against the obvious explanation that the latter observation is caused solely by cellular leakage.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Saa3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Amyloid A Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
151
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pubmed:geneSymbol |
SAA3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1535-47
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8335946-Amino Acid Sequence,
pubmed-meshheading:8335946-Animals,
pubmed-meshheading:8335946-Base Sequence,
pubmed-meshheading:8335946-Carrier Proteins,
pubmed-meshheading:8335946-Cell Line,
pubmed-meshheading:8335946-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:8335946-Gene Expression,
pubmed-meshheading:8335946-Lipopolysaccharides,
pubmed-meshheading:8335946-Macrophage Activation,
pubmed-meshheading:8335946-Macrophages,
pubmed-meshheading:8335946-Mice,
pubmed-meshheading:8335946-Molecular Sequence Data,
pubmed-meshheading:8335946-Oligodeoxyribonucleotides,
pubmed-meshheading:8335946-Peptide Fragments,
pubmed-meshheading:8335946-RNA, Messenger,
pubmed-meshheading:8335946-Serum Amyloid A Protein
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pubmed:year |
1993
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pubmed:articleTitle |
Identification by microsequencing of lipopolysaccharide-induced proteins secreted by mouse macrophages.
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pubmed:affiliation |
Innogenetics N.V., Industripark Zwijnaarde, Belgium.
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pubmed:publicationType |
Journal Article,
In Vitro
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