Expression, proteolysis and activation of caspases 6 and 7 during rat C6 glioma cell apoptosis

• Published in: Neuroscience letters 2002-05, Vol.324 (1), p.33-36
• Main Authors: Meller, Robert, Skradski, Shana L., Simon, Roger P., Henshall, David C.
• Format: Article
• Language: English
• Subjects: Animals; Apoptosis - physiology; Biological and medical sciences; Brain; Brain - enzymology; Brain - physiopathology; Brain Diseases - enzymology; Brain Diseases - physiopathology; Caspase 3; Caspase 6; Caspase 7; Caspases - metabolism; Enzyme Inhibitors - pharmacology; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Enzymologic - physiology; Glia; Glioma; In Situ Nick-End Labeling; Isolated neuron and nerve. Neuroglia; Lamin Type A; Lamins; Neurogeneration; Neuroglia - enzymology; Neuroglia - pathology; Neuron; Nuclear Proteins - metabolism; Peptide Hydrolases - metabolism; Rat; Rats; Staurosporine - pharmacology; Tumor Cells, Cultured; Vertebrates: nervous system and sense organs
• ISSN: 0304-3940; 1872-7972
• DOI: 10.1016/S0304-3940(02)00166-0

Activation of cysteinyl aspartate-specific proteases (caspases) may underlie apoptotic cell death in brain. Terminal, executioner caspases 3, 6 and 7 likely contribute to such cell death in a stimulus- and cell type-specific manner. Here we investigate the processing and activation of caspases 3, 6 and 7 in rat C6 glioma cells induced to undergo apoptosis by staurosporine (STS) treatment as a model of apoptosis in glia. Proteolysis and activation of caspases 3 and 7 as determined by immunoblotting and substrate-specific cleavage assay (DEVDase) preceded caspase-6 proteolysis and increased VEIDase activity following STS treatment. Activation of caspase-6 was paralleled by cleavage of the nuclear envelope protein lamin-A. These results highlight temporal differences in the activation of the triad of executioner caspases 3, 6 and 7 during glial cell apoptosis.