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Altered Na,K-ATPase pattern in gamma-crystallin mutant mice.
Invest Ophthalmol Vis Sci. 2002 May; 43(5):1517-9.IO

Abstract

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 alpha1, alpha2, and alpha3 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 alpha1, alpha2, and alpha3.

RESULTS

For the Na,K-ATPase isoforms alpha2 and alpha3, 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 alpha1 Na,K-ATPase isoform band density was also detected in lens material from the homozygous mutant mice. The Na,K-ATPase alpha3 polypeptide was also detected in lens membrane material obtained from heterozygous mice of both mutant strains. The alpha2 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 alpha1, alpha2, and alpha3 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 alpha2 and alpha3 isoform proteins of Na,K-ATPase is markedly upregulated in the cataractous lens.

Authors+Show Affiliations

Department of Ophthalmology and Visual Sciences, School of Medicine, University of Louisville, 301 E. Muhammad Ali Boulevard, Louisville, KY 40292, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

11980868

Citation

Moseley, Amy, et al. "Altered Na,K-ATPase Pattern in Gamma-crystallin Mutant Mice." Investigative Ophthalmology & Visual Science, vol. 43, no. 5, 2002, pp. 1517-9.
Moseley A, Graw J, Delamere NA. Altered Na,K-ATPase pattern in gamma-crystallin mutant mice. Invest Ophthalmol Vis Sci. 2002;43(5):1517-9.
Moseley, A., Graw, J., & Delamere, N. A. (2002). Altered Na,K-ATPase pattern in gamma-crystallin mutant mice. Investigative Ophthalmology & Visual Science, 43(5), 1517-9.
Moseley A, Graw J, Delamere NA. Altered Na,K-ATPase Pattern in Gamma-crystallin Mutant Mice. Invest Ophthalmol Vis Sci. 2002;43(5):1517-9. PubMed PMID: 11980868.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Altered Na,K-ATPase pattern in gamma-crystallin mutant mice. AU - Moseley,Amy, AU - Graw,Jochen, AU - Delamere,Nicholas A, PY - 2002/5/1/pubmed PY - 2002/6/4/medline PY - 2002/5/1/entrez SP - 1517 EP - 9 JF - Investigative ophthalmology & visual science JO - Invest Ophthalmol Vis Sci VL - 43 IS - 5 N2 - 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 alpha1, alpha2, and alpha3 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 alpha1, alpha2, and alpha3. RESULTS: For the Na,K-ATPase isoforms alpha2 and alpha3, 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 alpha1 Na,K-ATPase isoform band density was also detected in lens material from the homozygous mutant mice. The Na,K-ATPase alpha3 polypeptide was also detected in lens membrane material obtained from heterozygous mice of both mutant strains. The alpha2 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 alpha1, alpha2, and alpha3 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 alpha2 and alpha3 isoform proteins of Na,K-ATPase is markedly upregulated in the cataractous lens. SN - 0146-0404 UR - https://www.unboundmedicine.com/medline/citation/11980868/Altered_NaK_ATPase_pattern_in_gamma_crystallin_mutant_mice_ L2 - https://iovs.arvojournals.org/article.aspx?volume=43&issue=5&page=1517 DB - PRIME DP - Unbound Medicine ER -