ArticleNeurochemical research2000
Post-translational arginylation of proteins in cultured cells.
Article in Neurochemical research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Protein Arginylation: Milestones of Discovery.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Assaying the Posttranslational Arginylation of Proteins in Cultured Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase.International journal of molecular sciences · 2022Article
- Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
- Posttranslational arginylation as a global biological regulator.Developmental biology · 2011Review
- Arginylation-dependent neural crest cell migration is essential for mouse development.PLoS genetics · 2010Article
- Arginyltransferase regulates alpha cardiac actin function, myofibril formation and contractility during heart development.Development (Cambridge, England) · 2008Article
- Global analysis of posttranslational protein arginylation.PLoS biology · 2007Article
- Protein arginylation in rat brain cytosol: a proteomic analysis.Neurochemical research · 2006Article
- Re-examination of the post-translational arginylated protein of 125-kD initially identified as N-STOP.Neurochemical research · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of this study was to analyze the N-terminal post-translational incorporation of arginine into cytosolic proteins from cultured cells and the in vitro incorporation of arginine into soluble proteins of PC12 cells after serum deprivation. Arginine incorporation was measured in the presence of protein synthesis inhibitors. None of the inhibitors used affected significantly the arginylation reaction while the novo synthesis of protein was reduced by 98%. Under these conditions, we found that of the total [14C]arginine incorporated into the proteins, around 20% to 40% was incorporated into the N-terminal position of soluble proteins by a post-translational mechanism. These results suggest that this post-translational aminoacylation may be a widespread reaction in neuronal and non-neuronal cells. We also found that in PC12 cells, the in vitro post-translational arginylation was 60% higher in apoptotic cells with respect to control cells. These findings suggest that the post-translational arginylation of proteins may be involved in programmed cell death.
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Registered trials
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