ER stress does not cause upregulation and activation of caspase-2 to initiate apoptosis |
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| Authors: | J J Sandow L Dorstyn L A O'Reilly M Tailler S Kumar A Strasser P G Ekert |
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| Institution: | 1.The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia;2.Department of Medical Biology, The University of Melbourne, Parkville, VIC 3052, Australia;3.The Centre for Cancer Biology, SA Pathology, Adelaide, SA 5000, Australia;4.Department of Medicine, University of Adelaide, Adelaide, SA 5005, Australia;5.Division of Health Sciences, University of South Australia, Adelaide, SA 5001, Australia |
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| Abstract: | A recent report claimed that endoplasmic reticulum (ER) stress activates the ER trans-membrane receptor IRE1α, leading to increased caspase-2 levels via degradation of microRNAs, and consequently induction of apoptosis. This observation casts caspase-2 into a central role in the apoptosis triggered by ER stress. We have used multiple cell types from caspase-2-deficient mice to test this hypothesis but failed to find significant impact of loss of caspase-2 on ER-stress-induced apoptosis. Moreover, we did not observe increased expression of caspase-2 protein in response to ER stress. Our data strongly argue against a critical role for caspase-2 in ER-stress-induced apoptosis. |
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| Keywords: | caspase-2 ER stress apoptosis |
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