Retinal proteins were isolated simultaneously with RNA (Tri-Reagent; Sigma-Aldrich, Poole, UK). After processing, samples were solubilized in buffer with protease inhibitors (20 mM Tris-HCl [pH 7.4], containing 2 mM EDTA, 0.5 mM EGTA, 1% SDS, 0.1 mM phenylmethylsulfonyl fluoride, 50 μg/mL aprotinin, 50 μg/mL leupeptin, and 50 μg/mL pepstatin A). An equal volume of sample buffer (62.5 mM Tris-HCl [pH 7.4] containing 4% SDS, 10% glycerol, 10% β-mercaptoethanol, and 0.002% bromophenol blue) was then added. Electrophoresis of samples was performed with 10% polyacrylamide gels, containing 0.1% SDS, and the proteins were blotted onto activated ECL paper (GE Healthcare, Little Chalfont, UK). Blots were incubated for 3 hours at room temperature with primary antibodies against actin (monoclonal antibody, 1:1,000; Chemicon, Chandler’s Ford, UK), MCT1 (polyclonal anti-rabbit 1:10,000; Chemicon), MCT2 (polyclonal chicken, 1:1,000; Chemicon UK), MCT4 (1:100 polyclonal goat; Santa Cruz Biotechnology, Santa Cruz, CA), bFGF (polyclonal rabbit, 1:200; Santa Cruz Biotechnology), glial fibrillary acidic protein (GFAP; polyclonal rabbit, 1:400; Dako, Ely, UK), and activated caspase 3 (monoclonal antibody, 1:500; BD Biosciences, Cowley, UK). Blots were then incubated with appropriate secondary antibodies conjugated to horseradish peroxidase (1:5000, Sigma-Aldrich). Proteins were visualized by adding the chemiluminescent reagent (ECL; GE Healthcare) to the blots for 1 minute, and the intensity of the fluorescence recorded on high-sensitivity ECL film (GE Healthcare). The resultant bands’ intensity was quantified by computer (LabWorks software; UVP, Inc., Upland, CA).