| pubmed-article:9742106 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9742106 | lifeskim:mentions | umls-concept:C0040682 | lld:lifeskim |
| pubmed-article:9742106 | lifeskim:mentions | umls-concept:C0217250 | lld:lifeskim |
| pubmed-article:9742106 | lifeskim:mentions | umls-concept:C0021665 | lld:lifeskim |
| pubmed-article:9742106 | lifeskim:mentions | umls-concept:C1519315 | lld:lifeskim |
| pubmed-article:9742106 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:9742106 | pubmed:dateCreated | 1998-11-5 | lld:pubmed |
| pubmed-article:9742106 | pubmed:abstractText | To investigate the potential role of protein kinase C-delta (PKC-delta) in insulin-like growth factor I receptor (IGF-IR)-mediated cell transformation, an oncogenic gag-IGF-IR beta-fusion receptor lacking the entire extracellular domain, which was designated NM1, and a full-length IGF-IR were coexpressed with either wild-type PKC-delta (PKC-deltaWT) or an ATP-binding mutant of PKC-delta (PKC-deltaK376R) in NIH 3T3 fibroblasts. While overexpression of PKC-deltaWT did not affect NM1- and IGF-IR-induced focus and colony formation of NIH 3T3 cells, expression of PKC-deltaK376R severely impaired these events. In contrast, NM1-mediated cell growth in monolayer was not affected by coexpressing PKC-deltaK376R. PKC-deltaWT and PKC-deltaK376R were constitutively phosphorylated on a tyrosine residue(s) in the NM1- and IGF-IR-expressing cells and were associated with them in an IGF-I-independent manner. Activated IGF-IR was able to phosphorylate purified PKC-delta in vitro and stimulated its kinase activity. Furthermore, the level of endogenous PKC-delta protein was up-regulated through transcriptional activation in response to long-term IGF-IR activation. Taken together, our results demonstrate that PKC-delta plays an important role in IGF-IR-mediated cell transformation, probably via association of the receptor with PKC-delta and its activation through protein up-regulation and tyrosine phosphorylation. Competition with endogenous PKC-delta for NM1 and IGF-IR association by PKC-deltaK376R is probably an important mechanism underlying the PKC-deltaK376R-mediated inhibition of cell transformation by NM1 and IGF-IR. | lld:pubmed |
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| pubmed-article:9742106 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9742106 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9742106 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9742106 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9742106 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9742106 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9742106 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:KapoorVV | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:WangL HLH | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:LUCC | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:ZhangJJ | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:PierceJ HJH | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:JiangY XYX | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:SoonLL | lld:pubmed |
| pubmed-article:9742106 | pubmed:author | pubmed-author:FlechnerLL | lld:pubmed |
| pubmed-article:9742106 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9742106 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:9742106 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9742106 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9742106 | pubmed:pagination | 5888-98 | lld:pubmed |
| pubmed-article:9742106 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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