| pubmed-article:17227770 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C1418449 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C2698689 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C0031586 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C1565114 | lld:lifeskim |
| pubmed-article:17227770 | lifeskim:mentions | umls-concept:C1292733 | lld:lifeskim |
| pubmed-article:17227770 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17227770 | pubmed:dateCreated | 2007-3-19 | lld:pubmed |
| pubmed-article:17227770 | pubmed:abstractText | Phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes (PED/PEA)-15 is an anti-apoptotic protein whose expression is increased in several cancer cells and following experimental skin carcinogenesis. Exposure of untransfected C5N keratinocytes and transfected HEK293 cells to phorbol esters (12-O-tetradecanoylphorbol-13-acetate (TPA)) increased PED/PEA-15 cellular content and enhanced its phosphorylation at serine 116 in a time-dependent fashion. Ser-116 --> Gly (PED(S116G)) but not Ser-104 --> Gly (PED(S104G)) substitution almost completely abolished TPA regulation of PED/PEA-15 expression. TPA effect was also prevented by antisense inhibition of protein kinase C (PKC)-zeta and by the expression of a dominant-negative PKC-zeta mutant cDNA in HEK293 cells. Similar to long term TPA treatment, overexpression of wild-type PKC-zeta increased cellular content and phosphorylation of WT-PED/PEA-15 and PED(S104G) but not of PED(S116G). These events were accompanied by the activation of Ca2+-calmodulin kinase (CaMK) II and prevented by the CaMK blocker, KN-93. At variance, the proteasome inhibitor lactacystin mimicked TPA action on PED/PEA-15 intracellular accumulation and reverted the effects of PKC-zeta and CaMK inhibition. Moreover, we show that PED/PEA-15 bound ubiquitin in intact cells. PED/PEA-15 ubiquitinylation was reduced by TPA and PKC-zeta overexpression and increased by KN-93 and PKC-zeta block. Furthermore, in HEK293 cells expressing PED(S116G), TPA failed to prevent ubiquitin-dependent degradation of the protein. Accordingly, in the same cells, TPA-mediated protection from apoptosis was blunted. Taken together, our results indicate that TPA increases PED/PEA-15 expression at the post-translational level by inducing phosphorylation at serine 116 and preventing ubiquitinylation and proteosomal degradation. | lld:pubmed |
| pubmed-article:17227770 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17227770 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17227770 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17227770 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17227770 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17227770 | pubmed:author | pubmed-author:PerfettiAnnaA | lld:pubmed |
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| pubmed-article:17227770 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17227770 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:17227770 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17227770 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17227770 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17227770 | pubmed:pagination | 8648-57 | lld:pubmed |
| pubmed-article:17227770 | pubmed:dateRevised | 2009-4-7 | lld:pubmed |
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| pubmed-article:17227770 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17227770 | pubmed:articleTitle | Phorbol esters induce intracellular accumulation of the anti-apoptotic protein PED/PEA-15 by preventing ubiquitinylation and proteasomal degradation. | lld:pubmed |
| pubmed-article:17227770 | pubmed:affiliation | Dipartimento di Biologia e Patologia cellulare e Molecolare (DBPCM), Federico II University of Naples, Via Pansini 5, 80131 Naples, Italy. | lld:pubmed |
| pubmed-article:17227770 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17227770 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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