Source:http://linkedlifedata.com/resource/pubmed/id/10723089
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2000-5-31
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| pubmed:abstractText |
PGG-Glucan is a soluble beta-glucan immunomodulator that enhances a variety of leukocyte microbicidal activities without activating inflammatory cytokines. Although several different cell surface receptors for soluble (and particulate) beta-glucans have been described, the signal transduction pathway(s) used by these soluble ligands have not been elucidated. Previously we reported that PGG-Glucan treatment of mouse BMC2.3 macrophage cells activates a nuclear factor kappa-B-like (NF-kappaB) transcription factor complex containing subunit p65 (rel-A) attached to an unidentified cohort. In this study, we identify the cohort to be a non-rel family member: a CCAAT enhancer-binding protein-beta (C/EBP-beta)-related molecule with an apparent size of 48 kDa, which is a different protein than the previously identified C/EBP-beta p34 also present in these cells. C/EBP-beta is a member of the bZIP family whose members have previously been shown to interact with rel family members. This rel/bZIP heteromer complex activated by PGG-Glucan is different from the p65/p50 rel/rel complex induced in these cells by lipopolysaccharide (LPS). Thus, our data demonstrate that PGG-Glucan uses signal transduction pathways different from those used by LPS, which activates leukocyte microbicidal activities and inflammatory cytokines. We further show that heteromer activation appears to use protein kinase C (PKC) and protein tyrosine kinase (PTK) pathways, but not mitogen-activated protein kinase p38. Inhibitor kappa-B-alpha (IkappaB-alpha) is associated with the heteromer; this association decreases after PGG-Glucan treatment. These data are consistent with a model whereby treatment of BMC2.3 cells with PGG-Glucan activates IkappaB-alpha via PKC and/or PTK pathways, permitting translocation of the rel-A/CEBP-beta heteromer complex to the nucleus and increases its DNA-binding affinity.
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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/Adjuvants, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/CCAAT-Enhancer-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Probes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucans,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor RelA,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Glucans,
http://linkedlifedata.com/resource/pubmed/chemical/poly-1-6-glucopyranosyl-1-3-glucopyr...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0730-2312
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2000 Wiley-Liss, Inc.
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| pubmed:issnType |
Print
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| pubmed:volume |
77
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
221-33
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:10723089-Adjuvants, Immunologic,
pubmed-meshheading:10723089-Animals,
pubmed-meshheading:10723089-Base Sequence,
pubmed-meshheading:10723089-CCAAT-Enhancer-Binding Proteins,
pubmed-meshheading:10723089-Cell Line,
pubmed-meshheading:10723089-DNA Probes,
pubmed-meshheading:10723089-DNA-Binding Proteins,
pubmed-meshheading:10723089-Glucans,
pubmed-meshheading:10723089-Macromolecular Substances,
pubmed-meshheading:10723089-Mice,
pubmed-meshheading:10723089-Monocytes,
pubmed-meshheading:10723089-NF-kappa B,
pubmed-meshheading:10723089-Nuclear Proteins,
pubmed-meshheading:10723089-Protein Kinase C,
pubmed-meshheading:10723089-Protein-Tyrosine Kinases,
pubmed-meshheading:10723089-Signal Transduction,
pubmed-meshheading:10723089-Transcription Factor RelA,
pubmed-meshheading:10723089-Transcription Factors,
pubmed-meshheading:10723089-beta-Glucans
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| pubmed:year |
2000
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| pubmed:articleTitle |
Activation of a rel-A/CEBP-beta-related transcription factor heteromer by PGG-glucan in a murine monocytic cell line.
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| pubmed:affiliation |
Department of Biology/Biotechnology, Worcester Polytechnic Institute, Worcester, Massachusetts 01609, USA. dadams@wpi.edu
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| pubmed:publicationType |
Journal Article
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