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Phosphoproteomic analysis of neuronal cell death by glutamate‐induced oxidative stress
Author(s) -
Kang Tae Hyuk,
Bae KwangHee,
Yu Minjung,
Kim WonKon,
Hwang HyangRan,
Jung Hyeyun,
Lee Phil Young,
Kang Sunghyun,
Yoon TaeSung,
Park Sung Goo,
Ryu Seong Eon,
Lee Sang Chul
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200601028
Subject(s) - programmed cell death , oxidative stress , microbiology and biotechnology , biology , oxidative phosphorylation , proteomics , biochemistry , chemistry , apoptosis , gene
Oxidative stress is one of the major causes of neuronal cell death in disorders such as perinatal hypoxia and ischemia. Protein phosphorylation is the most significant PTM of proteins and plays an important role in stress‐induced signal transduction. Thus, the analysis of alternative protein phosphorylation states which occur during oxidative stress‐induced cell death could provide valuable information regarding cell death. In this study, a reference phosphoproteome map of the mouse hippocampal cell line HT22 was constructed based on 125 spots that were identified by MALDI‐TOF or LC‐ESI‐Q‐TOF‐MS analysis. In addition, proteins of HT22 cells at various stages of oxidative stress‐induced cell death were separated by 2‐DE and alterations in phosphoproteins were detected by Pro‐Q Diamond staining. A total of 17 spots showing significant quantitative changes and seven newly appearing spots were identified after glutamate treatment. Splicing factor 2, peroxiredoxin 2, S100 calcium binding protein A11, and purine nucleoside phosphorylase were identified as up‐ or down‐regulated proteins. CDC25A, caspase‐8, and cyp51 protein appeared during oxidative stress‐induced cell death. The data in this study from phosphoproteomic analysis provide a valuable resource for the understanding of HT22 cell death mechanisms mediated by oxidative stress.