Extracted proteins (50 μg) obtained from each sample (HRMECs and retinas) were subjected to SDS-PAGE in a Bio-Rad miniature slab gel apparatus and electrophoretically transferred onto a nitrocellulose membrane. The membrane was blocked in a 5% fat-free dried-milk solution and incubated overnight with partially purified rat or human anti–IL-1β monoclonal antibody (mAb; Proteintech, Rosemont, IL, USA, 16806-1-AP; Abcam, Cambridge, UK, ab9722), anti–IL-6 mAb (Bioworld Technology, Saint Louis Park, MN, USA, BS6419), anti-P53 mAb (Proteintech, 10442-1-AP), anti-Bax mAb (Cell Signaling Technology, Danvers, MA, USA, 14796), anti-ANGPTL3 mAb (Proteintech, 11964-1-AP; Abcam, ab175288), anti-integrin αV mAb (Abcam, ab150361), and integrin β3 mAb (Proteintech, 18309-1-AP). β-actin levels were detected using a mAb (Sigma-Aldrich, St. Louis, MO, USA, A2066) and used as an internal control to confirm equivalent total protein loading. Signal intensities in the control lanes were arbitrarily assigned a value of 1.0. Western blots were repeated three to five times.