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Papers In Press, published online ahead of print February 27, 2002
Department of Pathology, Children's Hospital, Boston, MA 02115
Corresponding Author: tcollins{at}rics.bwh.harvard.edu
Hydrogen peroxide (H2O2) has been implicated as a signaling agent in numerous signal transduction pathways in mammalian cells. However, to date, no sensor for low concentrations (<10 mM) of H2O2 has been identified. Using a functional proteomic approach, nuclear extracts from human umbilical vein endothelial cells (HUVECs) were analyzed by 2-dimensional polyacrylamide gel electrophoresis (2D-PAGE) with or without prior treatment with a low concentration of H2O2. A protein doublet with a MW of 39-41 kDa and an isoelectric point (pI) of ~5.0 was observed to be consistently altered by the treatment. Using proteolytic peptide mass fingerprinting, the protein was identified as heterogeneous nuclear ribonucleoprotein C1/C2 (hnRNP-C1/C2), a nuclear-restricted, pre-mRNA binding protein. By 2D-PAGE, each hnRNP-C splice-form is present as multiple spots, due to differing levels of phosphorylation. Upon treatment with H2O2, there is an increase in phosphorylation at 10-20 min, which partially reverses by 30 min. Subsequently at 60 min after treatment, a population of unphosphorylated protein is transiently present. The effects are observed with as little as 1 mM H2O2 and are maximal with 5-8 mM H2O2. The H2O2-stimulated phosphorylation was inhibited by catalase but was not inhibited by the transcriptional inhibitor actinomysin D.
J. Biol. Chem, 10.1074/jbc.M112153200
Submitted on December 19, 2001
Revised on February 25, 2002
Accepted on February 26, 2002
Rapid phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to physiologic levels of hydrogen peroxide in human endothelial cells
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