| pubmed-article:21094180 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21094180 | lifeskim:mentions | umls-concept:C0035322 | lld:lifeskim |
| pubmed-article:21094180 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:21094180 | lifeskim:mentions | umls-concept:C0010422 | lld:lifeskim |
| pubmed-article:21094180 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:21094180 | pubmed:dateCreated | 2010-12-21 | lld:pubmed |
| pubmed-article:21094180 | pubmed:abstractText | Protein phosphorylations have essential regulatory roles in visual signaling. Previously, we found that phosphorylation of several proteins in the retina and retinal pigment epithelium (RPE) is involved in anti-apoptotic signaling under oxidative stress conditions, including light exposure. In this study, we used a phosphoprotein enrichment strategy to evaluate the light-induced phosphoproteome of primary bovine RPE cells. Phosphoprotein-enriched extracts from bovine RPE cells exposed to light or dark conditions for 1h were separated by 2D SDS-PAGE. Serine and tyrosine phosphorylations were visualized by 2D phospho Western blotting and specific phosphorylation sites were analyzed by tandem mass spectrometry. Light induced a marked increase in tyrosine phosphorylation of beta crystallin A3 and A4. The most abundant light-induced up-regulated phosphoproteins were crystallins of 15-25 kDa, including beta crystallin S and zeta crystallin. Phosphorylation of beta crystallin suggests an anti-apoptotic chaperone function of crystallins in the RPE. Other chaperones, cytoskeletal proteins, and proteins involved in energy balance were expressed at higher levels in the dark. A detailed analysis of RPE phosphoproteins provides a molecular basis for understanding of light-induced signal transduction and anti-apoptosis mechanisms. Our data indicates that phosphorylation of crystallins likely represents an important mechanism for RPE shielding from physiological and pathophysiological light-induced oxidative injury. | lld:pubmed |
| pubmed-article:21094180 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21094180 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21094180 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21094180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21094180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21094180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21094180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21094180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21094180 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21094180 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:21094180 | pubmed:issn | 1879-0003 | lld:pubmed |
| pubmed-article:21094180 | pubmed:author | pubmed-author:JahngWan... | lld:pubmed |
| pubmed-article:21094180 | pubmed:author | pubmed-author:LeeSung... | lld:pubmed |
| pubmed-article:21094180 | pubmed:author | pubmed-author:LeeHyunjuH | lld:pubmed |
| pubmed-article:21094180 | pubmed:author | pubmed-author:ChungHyewonH | lld:pubmed |
| pubmed-article:21094180 | pubmed:copyrightInfo | Copyright © 2010 Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:21094180 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21094180 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:21094180 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:21094180 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21094180 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21094180 | pubmed:pagination | 194-201 | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:meshHeading | pubmed-meshheading:21094180... | lld:pubmed |
| pubmed-article:21094180 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21094180 | pubmed:articleTitle | Light-induced phosphorylation of crystallins in the retinal pigment epithelium. | lld:pubmed |
| pubmed-article:21094180 | pubmed:affiliation | Department of Ophthalmology, University of South Carolina, Columbia, SC 29208, USA. | lld:pubmed |
| pubmed-article:21094180 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21094180 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
