Source:http://linkedlifedata.com/resource/pubmed/id/21094180
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2010-12-21
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Crystallins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Proteome
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1879-0003
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2010 Elsevier B.V. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
194-201
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pubmed:meshHeading |
pubmed-meshheading:21094180-Alkaline Phosphatase,
pubmed-meshheading:21094180-Animals,
pubmed-meshheading:21094180-Cattle,
pubmed-meshheading:21094180-Crystallins,
pubmed-meshheading:21094180-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:21094180-Light,
pubmed-meshheading:21094180-Phosphorylation,
pubmed-meshheading:21094180-Phosphoserine,
pubmed-meshheading:21094180-Phosphotyrosine,
pubmed-meshheading:21094180-Proteome,
pubmed-meshheading:21094180-Reproducibility of Results,
pubmed-meshheading:21094180-Retinal Pigment Epithelium,
pubmed-meshheading:21094180-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2011
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pubmed:articleTitle |
Light-induced phosphorylation of crystallins in the retinal pigment epithelium.
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pubmed:affiliation |
Department of Ophthalmology, University of South Carolina, Columbia, SC 29208, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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