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lüll Caspase-12 processing and fragment translocation into nuclei of tunicamycin-treated cells Fujita E; Kouroku Y; Jimbo A; Isoai A; Maruyama K; Momoi TCell Death Differ 2002[Oct]; 9 (10): 1108-14Excess endoplasmic reticulum (ER) stress induces processing of caspase-12, which is located in the ER, and cell death. However, little is known about the relationship between caspase-12 processing and cell death. We prepared antisera against putative caspase-12 cleavage sites (anti-m12D318 and anti-m12D341) and showed that overexpression of caspase-12 induced autoprocessing at D(318) but did not induce cell death. Mutation analysis confirmed that D(318) was a unique autoprocessing site. In contrast, tunicamycin, one of the ER stress stimuli, induced caspase-12 processing at the N-terminal region and the C-terminal region (both at D(318) and D(341)) and cell death. Anti-m12D318 and anti-m12D341 immunoreactivities were located in the ER of the tunicamycin-treated cells, and some immunoreactivities were located around and in the nuclei of the apoptotic cells. Thus, processing at the N-terminal region may be necessary for the translocation of processed caspase-12 into nuclei and cell death induced by ER stress. Some of the caspase-12 processed at the N-terminal and C-terminal regions may directly participate in the apoptotic events in nuclei.|Active Transport, Cell Nucleus/drug effects/*physiology[MESH]|Animals[MESH]|Antibodies/immunology[MESH]|COS Cells[MESH]|Caspase 12[MESH]|Caspases/genetics/*metabolism[MESH]|Catalytic Domain/drug effects/immunology[MESH]|Cell Nucleus/drug effects/*enzymology[MESH]|Endoplasmic Reticulum/drug effects/*enzymology[MESH]|Eukaryotic Cells/drug effects/*enzymology[MESH]|Gene Expression Regulation, Enzymologic/drug effects/physiology[MESH]|Immunohistochemistry[MESH]|Protein Structure, Tertiary/drug effects/genetics[MESH]|Receptors, Peptide/metabolism[MESH]|Recombinant Fusion Proteins/genetics[MESH]|Stress, Physiological/*enzymology/genetics[MESH]|Tunicamycin/pharmacology[MESH] |