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Proteomic identification and comparative analysis of asymmetrically arginine-methylated proteins in immortalized, young and senescent cells

Authors
Lim, YongchulHong, EunyoungKwon, DaehoLee, Eunil
Issue Date
Dec-2010
Publisher
WILEY-BLACKWELL
Keywords
Asymmetric arginine methylation; Cellular senescence; Molecular chaperones; RNA-binding proteins; Type I protein arginine methyltransferases
Citation
ELECTROPHORESIS, v.31, no.23-24, pp.3823 - 3833
Indexed
SCIE
SCOPUS
Journal Title
ELECTROPHORESIS
Volume
31
Number
23-24
Start Page
3823
End Page
3833
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/115164
DOI
10.1002/elps.201000361
ISSN
0173-0835
Abstract
Protein-arginine methylation is one of the modifications that yields mono and dimethyl (asymmetric or symmetric) arginine residues in proteins. Previously, we found that asymmetric arginine methylation is decreased proportionately with a decrease of cell proliferation potential of cells, and such arginine methylation is greatest in immortalized cells, followed by normal young cells, and lowest in replicatively senescent cells. Using an asymmetric dimethyl-arginine-specific antibody, we identified arginine-methylated proteins in these cell types by immunoprecipitation and 2-D immunoblotting followed by MS. As a result, arginine methylation of chaperone molecules and RNA-binding proteins was differentially regulated between immortalized or young cells and senescent cells. Immortalized cells had significantly higher levels of methyl-accepting proteins, such as cleavage stimulation factor 2 (CstF2) and heterogenous nuclear ribonucleoprotein (hnRNP) R, than young cells. However, senescent cells contained hypomethylaed CstF2, hnRNP K, and chaperone containing TCP1 subunit 7, as well as decreased hnRNP R level. Further, significant reduction of arginine modification in CstF2 and chaperone containing TCP1 subunit 7 was observed in prematurely senescent fibroblasts, induced by treatment with adenosine dialdehyde, a transmethylation inhibitor, or subcytotoxic concentration of H2O2. These results suggest that asymmetric modification of RNA-binding proteins and molecular chaperones plays an essential role in maintaining cell proliferation capability.
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