Abstract:
:The human lens crystallin gene CRYGC T5P is associated with Coppock-like cataract and has a phenotype of a dust-like opacity of the fetal lens nucleus and deep cortical region. Previous in vitro mutation studies indicate that the protein has changed conformation, solubility, and stability, which may make it susceptible to aggregation, as seen in cataractous lens and cell culture expression. To investigate the mechanisms leading to these events, we studied protein-protein interactions using confocal fluorescence resonance energy transfer (FRET) microscopy. The method detects protein-protein interactions in the natural environment of living cells. Crystallin genes (CRYGC T5P, CRYGC, and CRYAA) were fused to either the green fluorescence protein (GFP) or red fluorescence protein (DsRED or RFP) vector. Each of the following GFP-RFP (donor-acceptor) plasmid pairs was cotransfected into HeLa cells: gammaC-gammaC, gammaC-gammaCT5P, gammaCT5P-gammaCT5P, alphaA-gammaC, and alphaA-gammaCT5P. After culture, confocal fluorescence cell images were taken. Protein-protein interactions in the form of net FRET were evaluated. The confocal fluorescence images show that cells expressing T5P gammaC-crystallin contain many protein aggregates, but cells co-expressing with either gammaC- or alphaA-crystallin reduce the aggregation considerably. FRET determination indicates that gammaCT5P-gammaCT5P shows less protein-protein interaction than either gammaC-gammaC or gammaC-gammaCT5P. Cotransfection with alphaA-crystallin (alphaA-gammaC or alphaA-T5PgammaC) increases nFRET compared with gammaC-gammaC or gammaC-T5PgammaC. Our results demonstrate that T5P gammaC-crystallin shows more protein aggregates and less protein-protein interaction than WT gammaC-crystallin. Chaperone alphaA-crystallin can rescue T5P gammaC-crystallin from aggregation through increased protein interaction. The formation of congenital cataract may be due to reduced protein-protein interactions and increased aggregation from an insufficient amount of alpha-crystallin for protection.
journal_name
Exp Eye Resjournal_title
Experimental eye researchauthors
Liu BF,Song S,Hanson M,Liang JJdoi
10.1016/j.exer.2008.08.021subject
Has Abstractpub_date
2008-12-01 00:00:00pages
515-20issue
6eissn
0014-4835issn
1096-0007pii
S0014-4835(08)00286-8journal_volume
87pub_type
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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更新日期:1983-11-01 00:00:00
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journal_title:Experimental eye research
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1016/s0014-4835(89)80072-7
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1006/exer.1993.1158
更新日期:1993-11-01 00:00:00
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1016/j.exer.2005.12.007
更新日期:2006-07-01 00:00:00
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journal_title:Experimental eye research
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1016/j.exer.2018.10.002
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1016/j.exer.2010.01.004
更新日期:2010-05-01 00:00:00
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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更新日期:2002-09-01 00:00:00
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journal_title:Experimental eye research
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journal_title:Experimental eye research
pub_type: 杂志文章,评审
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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更新日期:2018-01-01 00:00:00
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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