Address of Corresponding Author

Ophthalmic Res 2006;38:24-28 (DOI: 10.1159/000088527)

  Key Words

• Lens membranes
• Connexin 46
• Connexin 50
• Gap junctions
• Cataract
• Selenite

  Abstract

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

Copyright © 2006 S. Karger AG, Basel

  Author Contacts

C.R. Fleschner, PhD
Department of Biochemistry, Kirksville College of Osteopathic Medicine
800 West Jefferson Street
Kirksville, MO 63501-1443 (USA)
Tel. +1 660 626 2761, Fax +1 660 626 2981, E-Mail cfleschner@atsu.edu

  Article Information

Received: December 23, 2004
Accepted after revision: April 12, 2005
Published online: September 26, 2005
Number of Print Pages : 5
Number of Figures : 4, Number of Tables : 0, Number of References : 22