Редактирование: CRYGS (раздел)

==Publications==

{{medline-entry
|title=Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/21436267
|abstract=To identify proteomic differences between age-related nuclear cataracts (ARNCs) and normal lens nuclei. Total solubilized proteins from ARNC lens nuclei with different grades were compared with normal controls by 2-D differential in-gel electrophoresis (2-D DIGE). Proteins with different abundances were identified by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Sodium dodecyl sulfate polyacrylamide gel electrophoresis ([[SDS]]-PAGE) and liquid chromatography tandem mass spectrometry (LC-MS/MS) analyses determined the compositions of high molecular weight (HMW; >200 kDa) aggregates found in ARNC lens nuclei. Western blot analysis was used to verify the changes in αA-crystallin and glyceraldehyde 3-phosphate dehydrogenase ([[GAPDH]]) levels. The 2-D differential in-gel electrophoresis results showed that nine proteins were significantly less abundant in lens nuclei from ARNC patients than in control lens nuclei. Six proteins (αA-, βA3-, βA4-, βB1-, and γD-crystallin and putative uncharacterized protein DKFZp434A0627 from the [[CRYGS]] family) tended to decrease as the cataract grade increased, while the other three proteins (αB-crystallin, [[GAPDH]], and retinal dehydrogenase 1) did not show such a tendency. [[SDS]]-PAGE showed decreased protein levels at ∼20 kDa in ARNC lenses but significantly increased levels at HMW (>200 kDa). Liquid chromatography tandem mass spectrometry analysis showed that the HMW aggregates derived largely from crystallins also contained filensin, phakinin, and carbonyl reductase 1. Of all the components, αA-crystallin accounted for the highest fraction. αA-, αB-, and γD-crystallin and DKFZp434A0627 were more prone to aggregate than other crystallins. The results show that crystallins, especially αA-crystallin, aggregate irreversibly during ARNC development. Some enzymes ([[GAPDH]], retinal dehydrogenase 1, and carbonyl reductase 1) may be involved in and/or accelerate this process.
|mesh-terms=* Aging
* Cataract
* Chromatography, Liquid
* Crystallins
* Electrophoresis, Polyacrylamide Gel
* Eye Proteins
* Humans
* Lens Nucleus, Crystalline
* Middle Aged
* Proteomics
* Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
* Tandem Mass Spectrometry
* Two-Dimensional Difference Gel Electrophoresis

|full-text-url=https://sci-hub.do/10.1167/iovs.10-7094
}}