Correction: Proteasome Dysfunction Mediates High Glucose-Induced Apoptosis in Rodent Beta Cells and Human Islets

Protein levels of cleaved caspase-3, cleaved PARP and actin were analyzed by Western blotting in INS-1E cells exposed to different glucose concentrations. Levels of polyubiquitinated proteins, CHOP protein -an endoplasmatic reticulum stress marker-, 20S-β5 protein -a proteasome subunit-, and actin were analyzed by Western blottin in INS-1E cells after 48 hours of culture either in 10 mM or 33 mM glucose. Levels of cleaved caspase-3, cleaved PARP, and actin were analyzed by Western blotting in INS-1E cells cultured with or without150 nM MG-132 at normal or high glucose concentrations. Quantitative analysis of bands densities normalized to actin from immunoblots as shown in A detecting cleaved caspase 3 or cleaved PARP in cells treated with 30, 150 or 500 nM MG-132 at optimal or high glucose concentrations.