| pubmed-article:2824656 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C0013081 | lld:lifeskim |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C0312418 | lld:lifeskim |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C0036667 | lld:lifeskim |
| pubmed-article:2824656 | lifeskim:mentions | umls-concept:C1516240 | lld:lifeskim |
| pubmed-article:2824656 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:2824656 | pubmed:dateCreated | 1987-12-30 | lld:pubmed |
| pubmed-article:2824656 | 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. | lld:pubmed |
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| pubmed-article:2824656 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2824656 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2824656 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2824656 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2824656 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2824656 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:2824656 | pubmed:author | pubmed-author:ScheurichPP | lld:pubmed |
| pubmed-article:2824656 | pubmed:author | pubmed-author:PfizenmaierKK | lld:pubmed |
| pubmed-article:2824656 | pubmed:author | pubmed-author:ThomaBB | lld:pubmed |
| pubmed-article:2824656 | pubmed:author | pubmed-author:MaxeinerBB | lld:pubmed |
| pubmed-article:2824656 | pubmed:author | pubmed-author:UnglaubRR | lld:pubmed |
| pubmed-article:2824656 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2824656 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2824656 | pubmed:volume | 166 | lld:pubmed |
| pubmed-article:2824656 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2824656 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2824656 | pubmed:pagination | 1788-97 | lld:pubmed |
| pubmed-article:2824656 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2824656 | pubmed:meshHeading | pubmed-meshheading:2824656-... | lld:pubmed |
| pubmed-article:2824656 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:2824656 | pubmed:articleTitle | Downregulation of tumor necrosis factor (TNF) sensitivity via modulation of TNF binding capacity by protein kinase C activators. | lld:pubmed |
| pubmed-article:2824656 | pubmed:affiliation | Klinische Arbeitsgruppe BRWTI, Max-Planck-Gesellschaft, Göttingen, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:2824656 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2824656 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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