Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9
- O'Reilly, LA; Ekert, P; Harvey, N; Marsden, V; Cullen, L; Vaux, DL; Hacker, G; Magnusson, C; Pakusch, M; Cecconi, F; Kuida, K; Strasser, A; Huang, DCS; Kumar, S;
Publication Year 2002-08, Volume 9, Issue #8, Page 832-841
- Journal Title
- CELL DEATH AND DIFFERENTIATION
- Publication Type
- Journal Article
- We have generated rat monoclonal antibodies that specifically recognise caspase-2 from many species, including mouse, rat and humans. Using these antibodies, we have investigated caspase-2 expression, subcellular localisation and processing. We demonstrate that caspase-2 is expressed in most tissues and cell types. Cell fractionation and immunohistochemistry experiments show that caspase-2 is found in the nuclear and cytosolic fractions, including a significant portion present in the Golgi complex. We found that caspase-2 is processed in response to many apoptotic stimuli but experiments with caspase-2 deficient mice demonstrated that it is not required for apoptosis of thymocytes or dorsal root ganglia (DRG) neurons in response to a variety of cytotoxic stimuli. Caspase-2 processing does not occur in thymocytes lacking Apaf-1 or caspase-9, suggesting that in this cell type, activation of caspase-2 occurs downstream of apoptosome formation.
- NATURE PUBLISHING GROUP
- CELL-CYCLE ENTRY; CYTOCHROME-C; NEDD2 PRECURSOR; DEATH; ACTIVATION; LOCALIZATION; PROTEASE; BCL-2; INHIBITION; COMPLEX
- Publisher's Version
- Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2002-08-01 12:00:00Last Modified: 0001-01-01 12:00:00