rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1987-12-30
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pubmed:abstractText |
The regulatory action of activators for protein kinase C on the specific binding capacity for recombinant human tumor necrosis factor alpha (TNF-alpha) was studied on various human cell lines. Phorbol myristate acetate (PMA) and oleyl acetyl glycerol (OAG) both are able to rapidly downregulate TNF-binding capacity of normal and malignant cells derived from various tissues. As PMA treatment did not enhance internalization of TNF-alpha-receptor complexes at 37 degrees C, and since OAG was able to downregulate TNF-binding capacity under conditions where internalization and shedding of receptor protein are prevented, we conclude that protein kinase C controls ligand affinity of the TNF-receptor protein, possibly via direct phosphorylation. Protein kinase C triggered downregulation of TNF-alpha-binding capacity concomitantly resulted in reduction of TNF-alpha sensitivity, as revealed from decreased cytotoxic action of TNF-alpha on L 929 cells and from inhibition of TNF-alpha-mediated enhancement of HLA class II antigen expression in Colo 205 cells. Restoration of TNF-binding capacity upon abrogation of protein kinase C stimulation leads to full recovery of TNF responsiveness, further supporting the close linkage of TNF-receptor expression and TNF sensitivity. These data suggest that regulation of TNF-binding capacity by protein kinase C is one of the cellular control mechanisms of TNF responsiveness.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-221835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-2433337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-2948902,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-2993471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-2994048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-2999773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3001529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3026394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3026955,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3029221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3029503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3030559,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3031163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3033642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3038218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3087891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3878923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3933111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-3933986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-6238627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2824656-6427923
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1007
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
166
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
1788-97
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2824656-Cell Survival,
pubmed-meshheading:2824656-Cells, Cultured,
pubmed-meshheading:2824656-Endocytosis,
pubmed-meshheading:2824656-Humans,
pubmed-meshheading:2824656-Protein Kinase C,
pubmed-meshheading:2824656-Receptors, Cell Surface,
pubmed-meshheading:2824656-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:2824656-Recombinant Proteins,
pubmed-meshheading:2824656-Tetradecanoylphorbol Acetate,
pubmed-meshheading:2824656-Tumor Cells, Cultured,
pubmed-meshheading:2824656-Tumor Necrosis Factor-alpha
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pubmed:year |
1987
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pubmed:articleTitle |
Downregulation of tumor necrosis factor (TNF) sensitivity via modulation of TNF binding capacity by protein kinase C activators.
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pubmed:affiliation |
Klinische Arbeitsgruppe BRWTI, Max-Planck-Gesellschaft, Göttingen, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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