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Purpose: To examine the foveal structure and vasculature in eyes with an idiopathic epiretinal membrane (ERM). Methods: Forty-nine eyes of 48 patients with an idiopathic ERM were studied. The superficial foveal avascular zone (FAZ) was measured by optical coherence tomography angiography (OCTA; RTVue XR Avanti, Optovue Inc., Fremont, CA), and the central foveal thickness (CFT) was measured by swept source OCT (DRI-OCT, Topcon, Japan). Twenty eyes underwent vitrectomy with internal limiting membrane (ILM) peeling, and the FAZ and CFT were evaluated pre- and postoperatively. Forty-nine eyes of 49 age-matched healthy subjects were also examined as control. Results: The FAZ in eyes with an ERM was significantly smaller than that of the control eyes (0.188±0.16 mm2 vs 0.328±0.14 mm2, P<0.01). The CFT in eyes with an ERM was significantly thicker than that of control eyes (315±0.14 μm vs 193±0.14 μm, P<0.01). The size of the FAZ was strongly correlated with the CFT (ERM, R = -0.753; control, R = -0.61, both P<0.01). The postoperative size of the FAZ was not significantly different from the preoperative size (0.115 mm2 vs 0.128 mm2, P = 0.17) but the CFT was significantly thinner (370 μm vs 288 μm, P<0.01) after the vitrectomy with ILM peeling in 20 eyes. Conclusions: The results indicate that an ERM might affect the morphology and vasculature of not only the inner but also the outer retina before and after vitrectomy with ILM peeling. The FAZ area might have been affected by the ILM peeling. [ABSTRACT FROM AUTHOR]

Anion exchanger 1 (AE1) is a 95 kDa glycoprotein that facilitates exchange across the erythrocyte plasma membrane. This transport activity resides in the 52 kDa C-terminal membrane domain (Gly361-Val911) predicted to span the membrane 14 times. To explore the role of tryptophan (Trp) residues in AE1 function, the seven endogenous Trp residues in the membrane domain were mutated individually to alanine (Ala) and phenylalanine (Phe). Expression levels, cell surface abundance, inhibitor binding and transport activities of the mutants were measured upon expression in HEK-293 cells. The seven Trp residues divided into three classes according the impact of mutations on the functional expression of AE1: Class 1, dramatically decreased expression (Trp492 and Trp496); Class 2, decreased expression by Ala substitution but not Phe (Trp648, Trp662 and Trp723); and Class 3, normal expression (Trp831 and Trp848). The results indicate that Trp residues play differential roles in AE1 expression and function depending on their location in the protein and that Trp mutants with low expression are misfolded and retained in the endoplasmic reticulum. [ABSTRACT FROM AUTHOR]