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rdf:type |
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lifeskim:mentions |
umls-concept:C0020538,
umls-concept:C0023545,
umls-concept:C0027950,
umls-concept:C0030685,
umls-concept:C0054878,
umls-concept:C0127400,
umls-concept:C0162337,
umls-concept:C0391871,
umls-concept:C0392747,
umls-concept:C0443172,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1332127,
umls-concept:C1420085,
umls-concept:C1424798,
umls-concept:C1963578
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pubmed:issue |
6
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pubmed:dateCreated |
2009-6-2
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pubmed:abstractText |
In humans, heparin-binding protein (HBP) and the potent chemotactic lipid leukotriene B(4) (LTB(4)) are important mediators of innate immune responses. Here we show that human neutrophils (PMNs) challenged with LTB(4) (30 s to 5 min) release HBP as determined by Western blot analysis. This response peaks at 100 nM of agonist and is mediated by the BLT1 receptor. Protein phosphatase-1 (30 microM) and wortmannin (0.5 microM) block the LTB(4)-mediated HBP release from PMNs, which suggests involvement of the 1-phosphatidylinositol 3-kinase intracellular pathway during degranulation. Furthermore, postsecretory supernatants from LTB(4)-stimulated PMNs induce intracellular calcium mobilization in endothelial cells in vitro and increase in vascular permeability in vivo, as assessed in a mouse model of pleurisy. Selective removal of HBP from the supernatant significantly reduces these activities attributing a key role to HBP in the LTB(4)-induced change in vascular permeability. This lipid-protein axis could offer novel opportunities for pharmacological intervention in key steps of the vascular response to inflammation.
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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/Androstadienes,
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/LTB4R protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/LTB4R2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Leukotriene B4,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine...,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Leukotriene B4,
http://linkedlifedata.com/resource/pubmed/chemical/cationic antimicrobial protein CAP...,
http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1530-6860
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1750-7
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pubmed:meshHeading |
pubmed-meshheading:19151333-Androstadienes,
pubmed-meshheading:19151333-Animals,
pubmed-meshheading:19151333-Antimicrobial Cationic Peptides,
pubmed-meshheading:19151333-Blood Proteins,
pubmed-meshheading:19151333-Capillary Permeability,
pubmed-meshheading:19151333-Carrier Proteins,
pubmed-meshheading:19151333-Cells, Cultured,
pubmed-meshheading:19151333-Endothelial Cells,
pubmed-meshheading:19151333-Enzyme Inhibitors,
pubmed-meshheading:19151333-Female,
pubmed-meshheading:19151333-Humans,
pubmed-meshheading:19151333-Leukotriene B4,
pubmed-meshheading:19151333-Matrix Metalloproteinase 9,
pubmed-meshheading:19151333-Mice,
pubmed-meshheading:19151333-Mice, Inbred C57BL,
pubmed-meshheading:19151333-N-Formylmethionine Leucyl-Phenylalanine,
pubmed-meshheading:19151333-Neutrophils,
pubmed-meshheading:19151333-Peroxidase,
pubmed-meshheading:19151333-Receptors, Leukotriene B4
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pubmed:year |
2009
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pubmed:articleTitle |
Leukotriene B4-induced changes in vascular permeability are mediated by neutrophil release of heparin-binding protein (HBP/CAP37/azurocidin).
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pubmed:affiliation |
Department of Medical Biochemistry and Biophysics, Division of Chemistry 2, Karolinska Institutet, S-171 77 Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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