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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1992-8-25
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pubmed:abstractText |
The biochemical mechanism(s) underlying the priming of the macrophage for an enhanced PMA-induced respiratory burst is not understood. Because the cellular receptor for PMA is thought to be protein kinase C (PKC), we have investigated the effects of priming agents on cellular PKC levels. Sonicates from unprimed bone marrow-derived macrophages (BMM) were found to contain PKC activity (309 +/- 51 pmol 32P-incorporated/mg/min; mean +/- SE, n = 17) as measured by the phospholipid-, diacylglycerol-, and calcium-dependent phosphorylation of histone. Exposure of BMM to priming agents such as TNF-alpha, LPS, and granulocyte/macrophage-CSF resulted in a significant increase in both histone-phosphorylating activity and levels of immunoreactive PKC protein in these cells. A minimum of 6-h exposure, with an increasing effect up to 48 h, was required for a detectable increase in PKC level. The activity from primed BMM, like that of the untreated cells, was predominantly cytosolic. The kinetics and concentration dependence of the priming agent-induced increase in the PKC content of BMM closely paralleled the enhancing effects of these agents on the PMA-stimulated respiratory burst. Furthermore, CSF-1, a cytokine that does not prime BMM, failed to increase PKC activity. We propose that the exposure of BMM to priming agents leads to an increase in the expression of a stimulatory isozyme(s) of PKC, resulting in an enhanced ability to mount a respiratory burst in response to stimulation with PMA.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Granulocyte-Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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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 |
149
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1016-22
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1634760-Animals,
pubmed-meshheading:1634760-Bone Marrow Cells,
pubmed-meshheading:1634760-Dose-Response Relationship, Drug,
pubmed-meshheading:1634760-Granulocyte-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:1634760-Lipopolysaccharides,
pubmed-meshheading:1634760-Macrophages,
pubmed-meshheading:1634760-Mice,
pubmed-meshheading:1634760-Mice, Inbred CBA,
pubmed-meshheading:1634760-Molecular Weight,
pubmed-meshheading:1634760-Phosphoproteins,
pubmed-meshheading:1634760-Protein Kinase C,
pubmed-meshheading:1634760-Respiratory Burst,
pubmed-meshheading:1634760-Time Factors,
pubmed-meshheading:1634760-Tumor Necrosis Factor-alpha
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pubmed:year |
1992
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pubmed:articleTitle |
Priming of the respiratory burst of bone marrow-derived macrophages is associated with an increase in protein kinase C content.
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pubmed:affiliation |
Department of Medicine, University of Melbourne, Royal Melbourne Hospital, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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