title: Age-related changes in the water-soluble lens protein composition of Wistar and accelerated-senescence OXYS rats.
abstract: OBJECTIVE
  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.
authors.affiliation: International Tomography Center SBRAS, Institutskaya 3a, Novosibirsk, Russia.
authors.forename: Lyudmila V
authors.initials: LV
authors.lastname: Kopylova
authors.forename: Ivan V
authors.initials: IV
authors.lastname: Cherepanov
authors.forename: Olga A
authors.initials: OA
authors.lastname: Snytnikova
authors.forename: Yuliya V
authors.initials: YV
authors.lastname: Rumyantseva
authors.forename: Nataliya G
authors.initials: NG
authors.lastname: Kolosova
authors.forename: Yuri P
authors.initials: YP
authors.lastname: Tsentalovich
authors.forename: Renad Z
authors.initials: RZ
authors.lastname: Sagdeev
mesh_terms: D019588:Aging, Premature / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002386:Cataract / Q000235:genetics / Q000378:metabolism* / Q000473:pathology; D004195:Disease Models, Animal; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D007908:Lens, Crystalline / Q000378:metabolism* / Q000473:pathology; D051381:Rats; D055647:Rats, Transgenic; D017208:Rats, Wistar; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012995:Solubility; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014867:Water; D038202:alpha-Crystallin A Chain / Q000235:genetics / Q000378:metabolism*; D038206:beta-Crystallin B Chain / Q000235:genetics / Q000378:metabolism*; D038222:gamma-Crystallins / Q000235:genetics / Q000378:metabolism*
chemical_list: D038202:alpha-Crystallin A Chain; D038206:beta-Crystallin B Chain; C113634:beta-crystallin B2; D038222:gamma-Crystallins; D014867:Water