HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Moseley, A. Articles by Delamere, N. A. Search for Related Content PubMed PubMed Citation Articles by Moseley, A. Articles by Delamere, N. A.

Altered Na,K-ATPase Pattern in -Crystallin Mutant Mice

¹ From the Department of Ophthalmology and Visual Sciences, University of Louisville, Louisville, Kentucky; the ² Department of Molecular Genetics, Biochemistry and Microbiology, University of Cincinnati, Cincinnati, Ohio; and ³ GSF-National Research Center for Environment and Health, Institute of Mammalian Genetics, Neuherberg, Germany.

PURPOSE. Na,K-adenosine triphosphatase (ATPase) activity is elevated in the lenses of murine cataract Cryge^t and Cryge^ns mutant mice. In the present study, the expression of Na,K-ATPase 1, 2, and 3 catalytic subunit polypeptides was examined in the lenses of these mutant mice.

METHODS. Membrane material was isolated from lenses and brain of 3-week-old wild-type mice, as well as heterozygous and homozygous mutant mice. Microsomal membranes were prepared by centrifugation of the homogenized material, and Na,K-ATPase polypeptides were detected by immunoblot analysis with antibodies directed against the Na,K-ATPase isoforms 1, 2, and 3.

RESULTS. For the Na,K-ATPase isoforms 2 and 3, membrane material obtained from the homozygous cataract mutants showed dense immunoblot bands that were not detected in material obtained from wild-type mice. An apparent increase of the 1 Na,K-ATPase isoform band density was also detected in lens material from the homozygous mutant mice. The Na,K-ATPase 3 polypeptide was also detected in lens membrane material obtained from heterozygous mice of both mutant strains. The 2 Na,K-ATPase polypeptide was observed in lens membrane material obtained from heterozygous Cryge^t mice, and a less dense band was detected in heterozygous Cryge^ns mice. Band densities of Na,K-ATPase subunits 1, 2, and 3 detected in brain membrane material were similar in both mutant and wild-type mice.

CONCLUSIONS. The immunoblot results suggest that the abundance of Na,K-ATPase polypeptide is increased in the lens of the cataract mouse mutant but is not altered in the brain. The expression of the 2 and 3 isoform proteins of Na,K-ATPase is markedly upregulated in the cataractous lens.