ArticleBrain research2013
Calpain cleaves methionine aminopeptidase-2 in a rat model of ischemia/reperfusion.
Article in Brain research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- The Role of TRPC6 in the Neuroprotection of Calycosin Against Cerebral Ischemic Injury.Scientific reports · 2017Article
- Calpain-1 Mediated Disorder of Pyrophosphate Metabolism Contributes to Vascular Calcification Induced by oxLDL.PloS one · 2015Article
- In vitro ischemia triggers a transcriptional response to down-regulate synaptic proteins in hippocampal neurons.PloS one · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Ischemic stroke results in multiple injurious signals within a cell including dysregulation of calcium homeostasis. Consequently, there is an increase in the enzymatic activity of the calpains, calcium dependent proteases that are thought to contribute to neuronal injury. In addition, cellular stress due to ischemia/reperfusion also triggers a decrease in protein translation through activation of the unfolded protein response (UPR). In the present study we found that methionine aminopeptidase 2 (MetAP2), a critical component of the translation initiation complex, is a calpain substrate. In vitro calpain assays demonstrated that while MetAP2 has autoproteolytic activity, calpain also produces a stable proteolytic fragment at 50kDa using recombinant MetAP2. This 50kDa fragment, in addition to a 57kDa fragment was present in in vitro digestions of rat brain homogenates. Production of these fragments was inhibited by calpastatin, the endogenous and specific inhibitor of calpain. Using an in vivo middle cerebral artery occlusion (MCAO) model only the 57kDa fragment of MetAP2 was observed. These data suggest that calpain activation in stroke may regulate MetAP2-mediated protein translation giving calpains a larger role in the cellular stress response than previously determined.
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Registered trials
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