https://transhumanist.ru/index.php?action=history&feed=atom&title=CRYGS 2026-10-31T19:26:36Z История изменений этой страницы в вики MediaWiki 1.43.6 https://transhumanist.ru/index.php?title=CRYGS&diff=5250&oldid=prev 2021-05-12T13:36:00Z

<p>Новая страница: «Gamma-crystallin S (Beta-crystallin S) (Gamma-S-crystallin) [CRYG8] ==Publications== {{medline-entry |title=Proteomic analysis of human age-related nuclear cata...»</p> <p><b>Новая страница</b></p><div>Gamma-crystallin S (Beta-crystallin S) (Gamma-S-crystallin) [CRYG8]<br /> <br /> ==Publications==<br /> <br /> {{medline-entry<br /> |title=Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei.<br /> |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/21436267<br /> |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; &gt;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 (&gt;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.<br /> |mesh-terms=* Aging<br /> * Cataract<br /> * Chromatography, Liquid<br /> * Crystallins<br /> * Electrophoresis, Polyacrylamide Gel<br /> * Eye Proteins<br /> * Humans<br /> * Lens Nucleus, Crystalline<br /> * Middle Aged<br /> * Proteomics<br /> * Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization<br /> * Tandem Mass Spectrometry<br /> * Two-Dimensional Difference Gel Electrophoresis<br /> <br /> |full-text-url=https://sci-hub.do/10.1167/iovs.10-7094<br /> }}</div>

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