IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by David, L. L.
Right arrow Articles by Shearer, T. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by David, L. L.
Right arrow Articles by Shearer, T. R.

Investigative Ophthalmology & Visual Science, Vol 25, 1275-1283, Copyright © 1984 by Association for Research in Vision and Ophthalmology

ARTICLES AND REPORTS

Calcium-activated proteolysis in the lens nucleus during selenite cataractogenesis

LL David and TR Shearer

A single injection of 20 mumol sodium selenite/kg body weight in 10-day- old rats caused severe nuclear cataract within 4 days. By 4 days postselenite injection, nuclear calcium levels increased from 0.4 to 6.8 mmol/kg lens dry weight. The purpose of these experiments was to determine if this calcium increase was associated with proteolysis specifically in the lens nuclear region. Sodium dodecyl sulfate polyacrylamide electrophoresis of lens nuclear proteins following selenite injection showed: loss of 30, 27, and 26 K molecular weight polypeptides in the soluble fraction, loss of 83, 52, 30, 27, and 26 K polypeptides in the insoluble fraction, and loss of the major 26 K membrane protein. Gel chromatography of nuclear soluble proteins indicated a decrease in beta H and beta L crystallins following selenite injection. Two-hour in vitro incubation of nuclear lens homogenates with calcium duplicated many of the proteolytic changes occurring in lenses in vivo following selenite injection. Calcium induced proteolysis in vitro was inhibited by EGTA, leupeptin, and iodoacetate but was not inhibited by phenylmethylsulfonyl fluoride. These properties are similar to calcium activated protease (CAP) from other tissues. Activation of CAP, and subsequent degradation of nuclear proteins, may be causes of selenite cataract.


This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
Y. Ueda, C. Fukiage, M. Shih, T. R. Shearer, and L. L. David
Mass Measurements of C-terminally Truncated {alpha}-Crystallins from Two-dimensional Gels Identify Lp82 as a Major Endopeptidase in Rat Lens
Mol. Cell. Proteomics, May 1, 2002; 1(5): 357 - 365.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Ma, C. Fukiage, Y. H. Kim, M. K. Duncan, N. A. Reed, M. Shih, M. Azuma, and T. R. Shearer
Characterization and Expression of Calpain 10. A NOVEL UBIQUITOUS CALPAIN WITH NUCLEAR LOCALIZATION
J. Biol. Chem., July 20, 2001; 276(30): 28525 - 28531.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1984 by the Association for Research in Vision and Ophthalmology