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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-7-28
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pubmed:abstractText |
The binding of a 34-kDa (mol. wt.) acylpoly(1,3)galactoside (APG) extracted from a membrane proteoglycan of Klebsiella pneumoniae to human blood leucocytes was investigated. APG is made of a long poly(1,3)galactose chain, a core-like region and a lipid moiety which comprises two glucosamine residues bound to a phosphate group and two beta OH myristic acids. Fluoresceinated APG was shown to bind preferentially to monocytes and to a lesser extent to polymorphonuclear neutrophils, as determined by flow cytometry. Binding of fluoresceinated APG was inhibited by unlabelled APG; it was concentration dependent, but not saturable, with rapid kinetics. It occurred at +4 degrees C but was markedly increased at 37 degrees C. It involved trypsin-sensitive molecules on the membrane of monocytes. Neither the parent proteoglycan nor lipopolysaccharide from K. pneumoniae or Salmonella minnesota competed for APG binding. A minor non-specific binding to lymphocytes, occurring predominantly on B cells, was observed. Unlike that of lipopolysaccharide, the APG binding was not blocked by polymyxin B sulphate. Interaction between the galactose chain of APG and the galactose receptor does not account for the binding of APG to monocytes because the galactose receptor (Mac-2) is expressed at high density on activated macrophages but not on monocytes. Despite its strong binding to human blood monocytes, APG displayed a much weaker activity than K. pneumoniae membrane proteoglycan with respect to induction of monocyte cytokine synthesis. When administered as a Technetium 99 conjugate, APG was shown to label inflammatory foci in experimental animals, and its property as a marker of macrophages is currently being evaluated in clinical trials.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Galactosides,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Polymyxin B,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0300-9475
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1615280-Binding, Competitive,
pubmed-meshheading:1615280-Galactosides,
pubmed-meshheading:1615280-Humans,
pubmed-meshheading:1615280-Kinetics,
pubmed-meshheading:1615280-Klebsiella pneumoniae,
pubmed-meshheading:1615280-Lymphocytes,
pubmed-meshheading:1615280-Monocytes,
pubmed-meshheading:1615280-Neuraminidase,
pubmed-meshheading:1615280-Neutrophils,
pubmed-meshheading:1615280-Oxidation-Reduction,
pubmed-meshheading:1615280-Polymyxin B,
pubmed-meshheading:1615280-Polysaccharides, Bacterial,
pubmed-meshheading:1615280-Proteoglycans,
pubmed-meshheading:1615280-Respiratory Burst,
pubmed-meshheading:1615280-Structure-Activity Relationship,
pubmed-meshheading:1615280-Temperature,
pubmed-meshheading:1615280-Trypsin
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pubmed:year |
1992
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pubmed:articleTitle |
Binding of a bacterial acylpoly(1,3)galactoside to human blood leucocytes.
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pubmed:affiliation |
Laboratory of Immunology, INSERM U80 CNRS URA 1177 UCBL, Hôpital E. Herriot, Lyon, France.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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