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Am J Physiol Cell Physiol (September 10, 2003). doi:10.1152/ajpcell.00174.2003
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Submitted on May 1, 2003
Accepted on September 2, 2003

The influence of Lyn kinase on Na,K-ATPase in porcine lens epithelium

Larry D Bozulic1, William L Dean1, and Nicholas A Delamere2*

1 Biochemistry & Molecular Biology, University of Louisville, Louisville, KY, USA
2 Ophthalmology & Visual Science, University of Louisville, Louisville, KY, USA; Pharmacology & Toxicology, University of Louisville, Louisville, KY, USA

* To whom correspondence should be addressed. E-mail: delamere{at}louisville.edu.

Na,K-ATPase is essential for the regulation of cytoplasmic Na+ and K+ levels in lens cells. Studies on the intact lens suggest activation of tyrosine kinases may inhibit Na,K-ATPase function. Here, we tested the influence of Lyn kinase, a Src-family member, on tyrosine phosphorylation and Na,K-ATPase activity in membrane material isolated from porcine lens epithelium. Western blot studies indicated the expression of Lyn in lens cells. When membrane material was incubated in ATP-containing solution containing partially purified Lyn kinase, Na,K-ATPase activity was reduced by ~38%. Lyn caused tyrosine phosphorylation of multiple protein bands. Immunoprecipitation and Western blot analysis showed Lyn treatment causes an increase in density of a 100 kDa phosphotyrosine band immunopositive for Na,K-ATPase {alpha}1 polypeptide. Incubation with protein tyrosine phosphatase (PTB-1B) reversed the Lyn-dependent tyrosine phosphorylation increase and the change in Na,K-ATPase activity. The results suggest that Lyn kinase treatment of a lens epithelium membrane preparation is able to bring about partial inhibition of Na,K-ATPase activity associated with tyrosine phosphorylation of multiple membrane proteins including the Na,K-ATPase {alpha}1 catalytic subunit.




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