| pubmed-article:15788406 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C0109317 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1705767 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C0010734 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C0031716 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1370600 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1366882 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1522290 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1157380 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1150579 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1333340 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1333192 | lld:lifeskim |
| pubmed-article:15788406 | lifeskim:mentions | umls-concept:C1705791 | lld:lifeskim |
| pubmed-article:15788406 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:15788406 | pubmed:dateCreated | 2005-5-30 | lld:pubmed |
| pubmed-article:15788406 | pubmed:abstractText | Surfactant deficiency contributes to acute lung injury and may result from the elaboration of bioactive lipids such as oxysterols. We observed that the oxysterol 22-hydroxycholesterol (22-HC) in combination with its obligate partner, 9-cis-retinoic acid (9-cis-RA), decreased surfactant phosphatidylcholine (PtdCho) synthesis by increasing phosphorylation of the regulatory enzyme CTP:phosphocholine cytidylyltransferase-alpha (CCTalpha). Phosphorylation of CCTalpha decreased its activity. 22-HC/9-cis-RA inhibition of PtdCho synthesis was blocked by PD98059 or dominant-negative ERK (p42 kinase). Overexpression of constitutively active MEK1, the kinase upstream of p42 kinase, increased CCTalpha phosphorylation. Expression of truncated CCTalpha mutants lacking proline-directed sites within the C-terminal phosphorylation domain partially blocked oxysterol-mediated inhibition of PtdCho synthesis. Mutagenesis of Ser315 within CCTalpha was both required and sufficient to confer significant resistance to 22-HC/9-cis-RA inhibition of PtdCho synthesis. A novel putative ERK-docking domain N-terminal to this phosphoacceptor site was mapped within the CCTalpha membrane-binding domain (residues 287-300). The results are the first demonstration of a physiologically relevant phosphorylation site and docking domain within CCTalpha that serve as targets for ERKs, resulting in inhibition of surfactant synthesis. | lld:pubmed |
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| pubmed-article:15788406 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15788406 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15788406 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15788406 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15788406 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15788406 | pubmed:author | pubmed-author:CarterA... | lld:pubmed |
| pubmed-article:15788406 | pubmed:author | pubmed-author:MallampalliRa... | lld:pubmed |
| pubmed-article:15788406 | pubmed:author | pubmed-author:RyanAlan JAJ | lld:pubmed |
| pubmed-article:15788406 | pubmed:author | pubmed-author:ZhouJimingJ | lld:pubmed |
| pubmed-article:15788406 | pubmed:author | pubmed-author:TephlyLinda... | lld:pubmed |
| pubmed-article:15788406 | pubmed:author | pubmed-author:AgassandianMa... | lld:pubmed |
| pubmed-article:15788406 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15788406 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:15788406 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15788406 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15788406 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15788406 | pubmed:pagination | 21577-87 | lld:pubmed |
| pubmed-article:15788406 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15788406 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15788406 | pubmed:articleTitle | Oxysterols inhibit phosphatidylcholine synthesis via ERK docking and phosphorylation of CTP:phosphocholine cytidylyltransferase. | lld:pubmed |
| pubmed-article:15788406 | pubmed:affiliation | Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City 52242, USA. | lld:pubmed |
| pubmed-article:15788406 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15788406 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15788406 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15788406 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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