Fig. 5.
Anti-OLF1 and anti-OLF2 degrade mutant myocilin through an apparent lysosomal pathway. A) Western blot analysis of the detergent-insoluble fraction from induced iHEKI477N cells treated with DMSO, the proteasomal inhibitor MG-132, or the lysosomal inhibitor Baf A1 for 24 h following transient transfection of anti-OLF1 (left) or anti-OLF2 (middle). Quantification of Western blots of insoluble myocilinI477N from two independent experiments, with SD compared to myocilin level in the absence of antibody within each treatment. *P < 0.05; ***P < 0.0001 relative density compared to myocilinI477N alone. B) Dot blot analysis of spent media fraction shows extremely low levels of secreted myocilinI477N across these experiments.

Anti-OLF1 and anti-OLF2 degrade mutant myocilin through an apparent lysosomal pathway. A) Western blot analysis of the detergent-insoluble fraction from induced iHEKI477N cells treated with DMSO, the proteasomal inhibitor MG-132, or the lysosomal inhibitor Baf A1 for 24 h following transient transfection of anti-OLF1 (left) or anti-OLF2 (middle). Quantification of Western blots of insoluble myocilinI477N from two independent experiments, with SD compared to myocilin level in the absence of antibody within each treatment. *P < 0.05; ***P < 0.0001 relative density compared to myocilinI477N alone. B) Dot blot analysis of spent media fraction shows extremely low levels of secreted myocilinI477N across these experiments.

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