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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Caspase 2 / genetics
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Caspase 2 / metabolism*
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Cysteine Endopeptidases / genetics
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Cysteine Endopeptidases / metabolism*
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Endoplasmic Reticulum / enzymology
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Endoplasmic Reticulum / genetics
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Endoplasmic Reticulum / metabolism
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Endoplasmic Reticulum Stress / physiology*
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Humans
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Mice
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Mice, Inbred C57BL
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Mice, Transgenic
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Thymocytes / enzymology
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Thymocytes / metabolism
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Up-Regulation
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bcl-2 Homologous Antagonist-Killer Protein / genetics
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bcl-2 Homologous Antagonist-Killer Protein / metabolism
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bcl-2-Associated X Protein / genetics
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bcl-2-Associated X Protein / metabolism
Substances
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Bak1 protein, mouse
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Bax protein, mouse
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bcl-2 Homologous Antagonist-Killer Protein
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bcl-2-Associated X Protein
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CASP2 protein, human
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Casp2 protein, mouse
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Caspase 2
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Cysteine Endopeptidases