| Accumulation of large protein fragments in prematurely senescent ARPE-19 cells. | |
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MedLine Citation:
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PMID: 19458325 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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PURPOSE: Senescence of retinal pigment epithelial (RPE) cells is a crucial event in the pathogenesis of age-related macular degeneration (AMD). This study was designed to improve the understanding of proteomic changes that underlie RPE senescence. Specifically, the levels of several protein fragments in prematurely senescent ARPE-19 cells were quantitatively compared with those in control cells. METHODS: Premature senescence of human ARPE-19 cells was induced by repeated treatments with 6 mM tert-butylhydroperoxide (tert-BHP). Whole senescent cells were then treated with deuterated D(3)-acrylamide, and control cells were treated with normal D(0)-acrylamide. The D(3) and D(0) samples were mixed at a 1:1 ratio, and the proteins were separated by FPLC (fast protein liquid chromatography) and 2D-PAGE (two-dimensional polyacrylamide gel electrophoresis). After in-gel trypsinolysis, the relative quantification of selected proteins and fragments in the senescent cells versus control ARPE-19 cells was achieved by calculating the ratio of signal intensities for the deuterated and normal forms of cysteine-containing labeled peptides in MALDI-MS (matrix-assisted laser desorption/ionization mass spectrometry) spectra. RESULTS: Several large fragments of typical cytosolic proteins, such as GAPDH, triosephosphate isomerase, and M2-type pyruvate kinase increased approximately two- to threefold in the prematurely senescent ARPE-19 cells. CONCLUSIONS: This study is the first demonstration that large fragments of cytosolic proteins can be accumulated in prematurely senescent ARPE-19 cells, the in vitro model of AMD. These data suggest that protein degradation processes are impaired in these cells and point to a new type of "waste" material in post-mitotic cells that may contribute to the senescent phenotype. |
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Authors:
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Wei-Li Liao; Illarion V Turko |
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Publication Detail:
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Type: Journal Article Date: 2009-05-20 |
Journal Detail:
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Title: Investigative ophthalmology & visual science Volume: 50 ISSN: 1552-5783 ISO Abbreviation: Invest. Ophthalmol. Vis. Sci. Publication Date: 2009 Oct |
Date Detail:
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Created Date: 2009-09-24 Completed Date: 2009-10-02 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7703701 Medline TA: Invest Ophthalmol Vis Sci Country: United States |
Other Details:
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Languages: eng Pagination: 4992-7 Citation Subset: IM |
Affiliation:
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Center for Advanced Research in Biotechnology, National Institute of Standards and Technology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Cell Aging
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drug effects,
physiology* Cells, Cultured Chromatography, Liquid Cytosol / metabolism Electrophoresis, Gel, Two-Dimensional Eye Proteins / metabolism* Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / metabolism* Humans Models, Biological Oxidative Stress / drug effects Peptide Fragments / metabolism* Phenotype Pyruvate Kinase / metabolism* Retinal Pigment Epithelium / metabolism* Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Triose-Phosphate Isomerase / metabolism* tert-Butylhydroperoxide / toxicity |
| Chemical | |
Reg. No./Substance:
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0/Eye Proteins; 0/Peptide Fragments; 75-91-2/tert-Butylhydroperoxide; EC 1.2.1.12/Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); EC 2.7.1.40/Pyruvate Kinase; EC 5.3.1.1/Triose-Phosphate Isomerase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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