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1 Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston 77555; 2 The Retina Foundation of the Southwest, Dallas 75231; 3 Department of Ophthalmology, University of Texas Southwestern, Dallas 75231; 4 Department of Ophthalmology and Visual Sciences, University of Texas Medical Branch, Galveston, Texas 77555; Departments of 5 Anatomy and 6 Physiology, Indiana University School of Medicine, Gary, Indiana 46408; and 7 Renal Division, Brigham and Women's Hospital, Harvard Institutes of Medicine, Boston, Massachusetts 02115
Retinal pigment epithelium (RPE) possesses regulated chloride channels that are crucial for transepithelial fluid and ion transport. At present, little is known about the molecular nature of chloride channels in human adult RPE (haRPE) or the effects of oxidative stress on membrane conductance properties. In the present study, we assessed ClC channel and cystic fibrosis transmembrane conductance regulator (CFTR) expression and membrane chloride conductance properties in haRPE cells. ClC-5, ClC-3, ClC-2, and CFTR mRNA expression was confirmed with RT-PCR analysis, and protein expression was detected with Western blot analysis and immunofluorescence microscopy. Whole cell recordings of primary cultures of haRPE showed an outwardly rectifying chloride current that was inhibited by the oxidant H2O2. The inhibitory effects of H2O2 were reduced in cultured human RPE cells that were incubated with precursors of glutathione synthesis or that were stably transfected to overexpress glutathione S-transferase. These findings indicate a possible role for ClC channels in haRPE cells and suggest possible redox modulation of human RPE chloride conductances.
immunocytochemistry; patch clamp; glutathione; glutathione S-transferase
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