Figure 11.
Protein-protein interaction of α-crystallin with methionine sulfoxide reductase A (MsrA) in retinas of patients with age-related macular degenetration and vascular endothelial growth factor (VEGF) in oxygen-induced retinopathy (OIR). (A) Immunohistochemical localization of αA-crystallin (red), αB-crystallin (red) and MsrA (green). Arrows indicate co-localization (yellow) of αA-crystallin or αB-crystallin and MsrA. *: Drusen. Bar indicates 50 microns. (B). Western blot for αB-crystallin, VEGF, and VEGF-R2 in anti–VEGF-A immunoprecipitates from wild-type and αB-crystallin KO mice at P12 and P17 in OIR. αB-Crystallin binds to VEGF-A at P12 and P17 in wild-type mice but not in αB-crystallin KO mice. Knockout of αB-crystallin does not affect VEGF-R2 binding to VEGF-A. (C). Localization of αB crystallin and VEGF in cultured RPE cells after hypoxia (a–d) -Expression of αB-crystallin and VEGF in cultured RPE cells after cobalt chloride (150 μM) treatment for 6 hr (b–d). Nuclei are identified with DAPI (a; blue); along with staining for αB-crystallin (b; red) and VEGF (c; green). Double staining for αB-crystallin and VEGF is seen in merged (d; yellow). Bar indicates 20 microns. Panel (A). Reproduced with permission from Sreekumar et al. Methionine sulfoxide reductase A: Structure, function and role in ocular pathology. World J. Biol. Chem.2011 2(184–192). Panels (B& C) “This research was originally published in Blood. Kase et al. alphaB-crystallin regulation of angiogenesis by modulation of VEGF. Blood 2010; 115: 3398–3406, © The American Society of Hematology.”