作者: C.R. Fleschner
DOI: 10.1159/000088527
关键词: Biochemistry 、 Phosphorylation 、 Gap junction 、 Cortex (botany) 、 Chemistry 、 Blot 、 Nucleus 、 Proteolysis 、 Molecular biology 、 Connexin 、 Selenium
摘要: The purpose of this work was to determine if the lens gap junction proteins connexin 46 (Cx46) and 50 (Cx50) were altered with development selenite-induced cataract. Cataracts induced in young Sprague-Dawley rats a single subcutaneous injection sodium selenite; age-matched uninjected served as controls. Membrane fractions isolated from homogenates cortex nucleus normal cataractous lenses by differential discontinuous sucrose gradient centrifugation. Aliquots urea-insoluble protein membrane analyzed quantitative densitometry Western blots probed antibodies Cx46 Cx50. A significant decrease more slowly migrating Cx46-reactive band, which represents phosphorylated Cx46, found major fraction lenses. There no difference amounts either or Cx50 associated selenite cataract any examined. These results suggest that alteration function (as evidenced change phosphorylation Cx46) may be cataract, but neither nor is subject well-characterized proteolysis model.