rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1989-4-3
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pubmed:abstractText |
Peritoneal macrophages of Lipopolysaccharide (LPS)-refractory C3H/HeJ mouse failed to express the mRNA coding interleukin 1 (IL-1) beta when stimulated by the Ca2+ ionophore A23187 or LPS, though macrophages of LPS-responsive C3H/He responded to these stimulants. These results suggest that the defect of the response in C3H/HeJ macrophages toward LPS stimulation may be related to the Ca2+-dependent signal pathway. The extracts from the C3H/HeJ macrophages showed normal activities of both protein kinase C (PKC) and calmodulin (CaM) in comparison with those from LPS-responsive C3H/He macrophages. However, one species of CaM-binding proteins could hardly be detected by the cross-linking assay with 125I-CaM in C3H/HeJ macrophages stimulated by LPS. These results suggest that the LPS-refractory site in C3H/HeJ macrophages is related to the lack of this CaM-binding protein, and the Ca2+-dependent CaM system may play an important role in the activation of cells by LPS.
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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/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fc
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
158
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
723-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2493248-Animals,
pubmed-meshheading:2493248-Ascitic Fluid,
pubmed-meshheading:2493248-Calcimycin,
pubmed-meshheading:2493248-Calcium,
pubmed-meshheading:2493248-Calmodulin,
pubmed-meshheading:2493248-Calmodulin-Binding Proteins,
pubmed-meshheading:2493248-Chromatography, High Pressure Liquid,
pubmed-meshheading:2493248-Egtazic Acid,
pubmed-meshheading:2493248-Gene Expression Regulation,
pubmed-meshheading:2493248-Interleukin-1,
pubmed-meshheading:2493248-Lipopolysaccharides,
pubmed-meshheading:2493248-Macrophage Activation,
pubmed-meshheading:2493248-Macrophages,
pubmed-meshheading:2493248-Mice,
pubmed-meshheading:2493248-Mice, Inbred C3H,
pubmed-meshheading:2493248-Mice, Mutant Strains,
pubmed-meshheading:2493248-Protein Kinase C,
pubmed-meshheading:2493248-RNA, Messenger,
pubmed-meshheading:2493248-Receptors, Fc
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pubmed:year |
1989
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pubmed:articleTitle |
Defect of calmodulin-binding protein in expression of interleukin-1 beta gene by LPS-nonresponder C3H/HeJ mouse macrophages.
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pubmed:affiliation |
Department of Microbiology, Jichi Medical School, Tochigi-ken, Japan.
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pubmed:publicationType |
Journal Article
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