Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
28
|
| pubmed:dateCreated |
1993-11-24
|
| pubmed:abstractText |
Binding of human recombinant interleukin-1 beta (IL-1 beta) to the cell surface receptors of EL-4 6.1 murine T-cells results in enhanced phosphorylation of several cellular proteins. Staurosporine abolished the enhanced phosphorylation in response to IL-1 for some of these proteins, suggesting that protein kinase C (PKC) was at least partially responsible. PKC-beta was translocated from the cytosol to the plasma membrane between 2 and 15 min after IL-1 binding. Activation of PKC-beta was enhanced by the protein phosphatase inhibitor okadaic acid. In fact, okadaic acid inhibited dephosphorylation of the PKC-specific peptide GS (Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ala-Ala-Lys-Lys). On the other hand, okadaic acid also led to elevation of IL-1-induced trans/autophosphorylation of PKC-beta. Accordingly, IL-1 induction of interleukin-2 synthesis was markedly enhanced by okadaic acid in EL-4 cells. These data suggest that activation of PKC-beta contributes to enhanced phosphorylation of cellular proteins in IL-1-treated cells and support the importance of protein phosphorylation and dephosphorylation in the regulation of IL-1-induced IL-2 synthesis in EL-4 6.1 T-cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ethers, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Okadaic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
268
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
21066-72
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8407943-Amino Acid Sequence,
pubmed-meshheading:8407943-Animals,
pubmed-meshheading:8407943-Biological Transport,
pubmed-meshheading:8407943-Cell Membrane,
pubmed-meshheading:8407943-Cells, Cultured,
pubmed-meshheading:8407943-Enzyme Activation,
pubmed-meshheading:8407943-Ethers, Cyclic,
pubmed-meshheading:8407943-Humans,
pubmed-meshheading:8407943-Interleukin-1,
pubmed-meshheading:8407943-Interleukin-2,
pubmed-meshheading:8407943-Mice,
pubmed-meshheading:8407943-Molecular Sequence Data,
pubmed-meshheading:8407943-Okadaic Acid,
pubmed-meshheading:8407943-Phosphoprotein Phosphatases,
pubmed-meshheading:8407943-Phosphorylation,
pubmed-meshheading:8407943-Protein Kinase C,
pubmed-meshheading:8407943-Signal Transduction,
pubmed-meshheading:8407943-T-Lymphocytes
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
Interleukin-1-induced signaling in T-cells. Evidence for the involvement of phosphatases PP1 and PP2A in regulating protein kinase C-mediated protein phosphorylation and interleukin-2 synthesis.
|
| pubmed:affiliation |
Institute of Molecular Pharmacology, Medical School of Hannover, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|