Regulation of Na,K-ATPase Function in the Lens

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Abstract

The two cell types in the lens, epithelium and fiber, have a very different specific activity of Na,K-ATPase; activity is much higher in the epithelium. However, judged by Western blot, fibers and epithelium express a similar amount of both Na,K-ATPase α and β subunit proteins. Na,K-ATPase protein abundance does not tally with Na,K-ATPase activity. Studies were conducted to examine whether protein synthesis plays a role in maintenance of the high Na,K-ATPase activity in lens epithelium. An increase of cytoplasmic sodium was found to increase Na,K-ATPase protein expression in the epithelium, but not in the fibers. The findings illustrate the ability of lens epithelium to synthesize new Na,K-ATPase protein as a way to boost Na,K-ATPase in response to cell damage or pathological events. Methionine incorporation studies suggested Na,K-ATPase synthesis may also play a role in day to day preservation of high Na,K-ATPase activity. Na,K-ATPase protein in lens epithelial cells appeared to be continually synthesized and degraded. Experiments with cycloheximide suggest that specific activity of Na,K-ATPase in the lens epithelium may depend on the ability of the cells to continuously synthesize fresh Na,K-ATPase proteins. However, other factors such as phosphorylation of Na,K-ATPase α subunit may also influence Na,K-ATPase activity. When intact lenses were exposed to the agonist thrombin, Na,K-ATPase activity was diminished, but the response was suppressed by inhibitors of the Src family of non-receptor tyrosine kinases. Thrombin elicited tyrosine phosphorylation of lens epithelium membrane proteins, including a 100 kDa protein band thought to be the Na,K-ATPase α 1 subunit. It remains to be determined whether a tyrosine phosphorylation mechanism contributes to the low activity of Na,K-ATPase in lens fibers.

Original languageEnglish (US)
Pages (from-to)25-29
Number of pages5
JournalJournal of Experimental Zoology Part A: Comparative Experimental Biology
Volume300
Issue number1
StatePublished - Nov 1 2003
Externally publishedYes

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sodium-potassium-exchanging ATPase
Lens
epithelium
tyrosine
phosphorylation
thrombin
proteins
protein synthesis

ASJC Scopus subject areas

  • Animal Science and Zoology

Cite this

Regulation of Na,K-ATPase Function in the Lens. / Delamere, Nicholas A.

In: Journal of Experimental Zoology Part A: Comparative Experimental Biology, Vol. 300, No. 1, 01.11.2003, p. 25-29.

Research output: Contribution to journalArticle

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