Tags

Type your tag names separated by a space and hit enter

The influence of Lyn kinase on Na,K-ATPase in porcine lens epithelium.
Am J Physiol Cell Physiol. 2004 Jan; 286(1):C90-6.AJ

Abstract

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 approximately 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 alpha1 polypeptide. Incubation with protein tyrosine phosphatase 1B (PTP-1B) reversed the Lyn-dependent tyrosine phosphorylation increase and the change of 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 alpha1 catalytic subunit.

Authors+Show Affiliations

Department of Ophthalmology and Visual Sciences, School of Medicine, University of Louisville, Louisville, KY 40202, 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

12967913

Citation

Bozulic, Larry D., et al. "The Influence of Lyn Kinase On Na,K-ATPase in Porcine Lens Epithelium." American Journal of Physiology. Cell Physiology, vol. 286, no. 1, 2004, pp. C90-6.
Bozulic LD, Dean WL, Delamere NA. The influence of Lyn kinase on Na,K-ATPase in porcine lens epithelium. Am J Physiol Cell Physiol. 2004;286(1):C90-6.
Bozulic, L. D., Dean, W. L., & Delamere, N. A. (2004). The influence of Lyn kinase on Na,K-ATPase in porcine lens epithelium. American Journal of Physiology. Cell Physiology, 286(1), C90-6.
Bozulic LD, Dean WL, Delamere NA. The Influence of Lyn Kinase On Na,K-ATPase in Porcine Lens Epithelium. Am J Physiol Cell Physiol. 2004;286(1):C90-6. PubMed PMID: 12967913.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The influence of Lyn kinase on Na,K-ATPase in porcine lens epithelium. AU - Bozulic,Larry D, AU - Dean,William L, AU - Delamere,Nicholas A, Y1 - 2003/09/10/ PY - 2003/9/12/pubmed PY - 2004/1/24/medline PY - 2003/9/12/entrez SP - C90 EP - 6 JF - American journal of physiology. Cell physiology JO - Am J Physiol Cell Physiol VL - 286 IS - 1 N2 - 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 approximately 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 alpha1 polypeptide. Incubation with protein tyrosine phosphatase 1B (PTP-1B) reversed the Lyn-dependent tyrosine phosphorylation increase and the change of 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 alpha1 catalytic subunit. SN - 0363-6143 UR - https://www.unboundmedicine.com/medline/citation/12967913/The_influence_of_Lyn_kinase_on_NaK_ATPase_in_porcine_lens_epithelium_ L2 - https://journals.physiology.org/doi/10.1152/ajpcell.00174.2003?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -