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Your search keyword '"Cherepanov, Ivan V."' showing total 2 results
Start Over Author "Cherepanov, Ivan V." Publisher molecular vision
2 results on '"Cherepanov, Ivan V."'

1. Cataract-specific posttranslational modifications and changes in the composition of urea-soluble protein fraction from the rat lens

Author

Yanshole, Lyudmila V., Cherepanov, Ivan V., Snytnikova, Olga A., Yanshole, Vadim V., Sagdeev, Renad Z., and Tsentalovich, Yuri P.

Subjects
Molecular Sequence Data, Acetylation, Chemical Fractionation, Crystallins, eye diseases, Cataract, Rats, Oxidative Stress, Solubility, Tandem Mass Spectrometry, Lens, Crystalline, Animals, Humans, Urea, Electrophoresis, Gel, Two-Dimensional, sense organs, Amino Acid Sequence, Amino Acids, Phosphorylation, Rats, Wistar, Eye Proteins, Oxidation-Reduction, Protein Processing, Post-Translational, Research Article
Abstract

Purpose To determine age-related changes in the composition of the urea-soluble (US) protein fraction from lenses of senescence-accelerated OXYS (cataract model) and Wistar (control) rats and to establish posttranslational modifications (PTMs) occurring under enhanced oxidative stress in OXYS lenses. Methods The identity and the relative abundance of crystallins in the US fractions were determined using two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption ionization–time of flight mass spectrometry (MS). The identities and the positions of PTMs were established using MS/MS measurements. Results Two-dimensional gel electrophoresis maps of US protein fractions were obtained for lenses of 3-, 12-, and 62-week-old Wistar and OXYS rats, and the relative abundance of different isoforms of α-, β-, and γ-crystallins was determined. β-Crystallins were the major contributor of the US fraction in 3-week-old lenses (above 50%), γ-crystallins in 12-week-old lenses (50–60%), and in 62-week-old lenses, the contributions from all three crystallin families leveled out. The major interstrain difference was the elevated level of α-crystallins in the US fraction from 12-week-old OXYS lenses. Spots with increased relative abundance in OXYS maps were attributed to the cataract-specific spots of interest. The crystallins from these spots were subjected to MS/MS analysis, and the positions of acetylation, oxidation, deamidation, and phosphorylation were established. Conclusions The increased relative abundance of α-crystallins in the US fraction from 12-week-old OXYS lenses points to the fast insolubilization of α-crystallins under oxidative stress. Most of the PTMs attributed to the cataract-specific modifications also correspond to α-crystallins. These PTMs include oxidation of methionine residues, deamidation of asparagine and glutamine residues, and phosphorylation of serine and threonine residues.

Published
2013

2. Age-related changes in the water-soluble lens protein composition of Wistar and accelerated-senescence OXYS rats.

Author

Kopylova LV, Cherepanov IV, Snytnikova OA, Rumyantseva YV, Kolosova NG, Tsentalovich YP, and Sagdeev RZ

Subjects
Aging, Premature genetics, Animals, Cataract genetics, Cataract pathology, Disease Models, Animal, Electrophoresis, Gel, Two-Dimensional, Humans, Lens, Crystalline pathology, Rats, Rats, Transgenic, Rats, Wistar, Reverse Transcriptase Polymerase Chain Reaction, Solubility, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Water, alpha-Crystallin A Chain genetics, beta-Crystallin B Chain genetics, gamma-Crystallins genetics, Aging, Premature metabolism, Cataract metabolism, Lens, Crystalline metabolism, alpha-Crystallin A Chain metabolism, beta-Crystallin B Chain metabolism, gamma-Crystallins metabolism
Abstract

Purpose: To determine the age-related and the cataract-specific changes in the crystallin composition in lenses of accelerated-senescence OXYS (cataract model) and Wistar (control) rats., Methods: The water soluble (WS) and insoluble (WIS) fractions of the lens proteins were separated; the identity and relative abundance of each crystallin in WS fraction were determined with the use of two-dimensional electrophoresis (2-DE) and Matrix-Assisted Laser Desorption Ionization-Time Of Flight (MALDI-TOF) mass spectrometry. All statistical calculations were performed using the software package Statistica 6.0 by factor dispersion analysis (ANOVA/MANOVA) and Newman-Keuls post-hoc test for comparison of group mean values., Results: The WIS protein content increased significantly in the aged animal lenses; the WIS/WS ratio increases in approximately 8 times to the age of 62 weeks. The interstrain difference was insignificant in this experiment. 2-DE maps of the young rat lenses (3 weeks) showed single spots for each lens protein while in older lenses (12 and 62 weeks) each crystallin was presented by several spots. The abundance of γA-γF-crystallins in WS fraction significantly decreases with age. A significant increase in the percentage abundance was also found for α-crystallins and βB2-crystallin from 3 to 12 weeks. The major differences between Wistar and OXYS lenses are the faster decay of the content of γA-γF-crystallins in OXYS lenses, and the significant decrease of unmodified αA-crystallin abundance in old OXYS lenses., Conclusions: The presented results demonstrate that the increase of the water-insoluble (WIS) protein fraction is rather age-specific than cataract-specific phenomenon. The major age-related changes in WS protein composition are the fast insolubilization of γ-crystallins, and the increase of αB- and βB2-crystallin abundance. The main interstrain differences, which could be attributed to the cataract-specific processes, are the faster decay of the content of γ-crystallins and the significant decrease of unmodified αA-crystallin abundance in the OXYS lenses.

Published
2011

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