Figure 5. Immunoprecipitation of TERT or ERα from normal and cataractous LEC lysates followed by immunoblotting with anti-Omni-Phos antibody or anti-pAkt antibody. A-C: Anti-Omni-phos® antibody detected nonspecific phosphorylation of ERα and TERT in both normal and cataractous LEC, though the immunoprecipitated TERT and ERα proteins were shown to be more highly phosphorylated in cataractous than in normal LEC. D-F: Anti-pAkt antibody revealed that pAkt interacts with ERα and TERT proteins in cataractous LEC but not in normal LEC. These findings imply that phosphorylation of TERT and ERα is Akt-dependent during cataractogenesis and that pAkt is not the kinase involved in normal LEC-telomerase activity. C=control; n=normal LEC; D and I=naturally occurring (diabetic or inherited) canine cataractous LEC; ER or ERα=estrogen receptor alpha; T=TERT. This experiment is representative of two repeated experiments. Statistical analysis was not performed.