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1 Biology, Indiana University - Purdue University at Indianapolis, Indianapolis, IN, USA
2 Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN, USA
* To whom correspondence should be addressed. E-mail: bblazer{at}iupui.edu.
ENaC-EGFP stably transfected clonal lines derived from the A6 parental cell line were used to study the physical mechanisms of insulin-stimulated Na+ transport. Within 1 minute of insulin stimulation, ENaC migrates from a diffuse cytoplasmic localization to the apical and lateral membranes. Concurrently, after insulin stimulation, phosphatidylinositol 3-kinase (PI3-kinase) is co-localized with ENaC on the lateral but not apical membrane. An inhibitor of PI3-kinase, LY294002, does not inhibit ENaC/PI3-kinase co-localization but does alter the intracellular site of the co-localization preventing the translocation of ENaC to the lateral and apical membranes. These data show that insulin stimulation causes the migration of ENaC to the lateral and apical cell membranes and this trafficking is dependent on PI3-kinase activity.
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