title: [Analysis of cytoskeletal proteins in rat selenium cataract using two-dimensional electrophoresis].
abstract: OBJECTIVE
  Previous studies used sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to characterize the modifications to lens proteins during opacification in the selenite model for cataract. To analyze the protein modifications in more detail, two dimensional electrophoresis (2 DE), which is more sensitive than 1 D electrophoresis, was used.
  
  
  RESULTS
  The results of 2 DE demonstrated rapid changes in cytoskeletal proteins including spectrin and vimentin at the earliest stages of opacification.
  
  
  CONCLUSIONS
  The results suggested that the mechanism of opacification might involve changes in cytoskeletal proteins during the earliest stages of cataract formation.
authors.affiliation: Department of Ophthalmology, Dokkyo University School of Medicine, Tochigi, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Matsushima
authors.forename: K
authors.initials: K
authors.lastname: Mukai
authors.forename: Y
authors.initials: Y
authors.lastname: Obara
authors.forename: J I
authors.initials: JI
authors.lastname: Clark
mesh_terms: D000818:Animals; D002386:Cataract / Q000139:chemically induced / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000032:analysis*; D015180:Electrophoresis, Gel, Two-Dimensional; D051381:Rats; D017207:Rats, Sprague-Dawley; D012643:Selenium; D013049:Spectrin / Q000032:analysis; D014746:Vimentin / Q000032:analysis
chemical_list: D003598:Cytoskeletal Proteins; D014746:Vimentin; D013049:Spectrin; D012643:Selenium