Proteomic analysis of the copper ion-induced stress response in a human embryonic carcinoma cell line.
Excessive exposure to copper, a redox-active metal, generates free radicals, which can cause cellular damage. In this study, we aim to identify the proteins that are up- or downregulated by copper exposure in human embryonic carcinoma (NCCIT) cells and to understand the mechanisms that play a role in the copper-induced stress response. After exposure to copper ions, the cells showed upregulated levels of 78 kDa glucose-regulated protein, fibrillin 1, CWC22 spliceosome-associated protein (KIAA1604), heat shock protein (HSP) 60, and HSP70, while the tumor necrosis factor receptor-associated factor 6, vimentin, 14-3-3 protein zeta, and RAC-beta (AKT2) serine/threonine protein kinase were downregulated. The GeneGo Process Networks of the proteins upregulated by copper ions were analyzed, and the 3 highest-scoring networks from the proteins upregulated by copper ions are presented here. In particular, the increased level of HSP70 in response to copper ions occurred in a dose-dependent manner, indicating that HSP70 could be a potential biomarker for copper toxicity in mammalian cells.
Division of Molecular and Life Science, Hanyang University, Ansan, Gyeonggido, Republic of Korea.
Dal Mu Ri
DM
Han
Mi Ran
MR
Choi
Kyoung Hwa
KH
Jung
Hyung Tae
HT
Lee
Ji Hyun
JH
Park
Takbum
T
Ohn
Young Gyu
YG
Chai
D048948:14-3-3 Proteins / Q000235:genetics / Q000378:metabolism; D015153:Blotting, Western; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D045744:Cell Line, Tumor; D002470:Cell Survival; D018834:Chaperonin 60 / Q000235:genetics / Q000378:metabolism; D003300:Copper / Q000633:toxicity*; D015536:Down-Regulation; D015180:Electrophoresis, Gel, Two-Dimensional; D000091342:Endoplasmic Reticulum Chaperone BiP; D000071838:Fibrillin-1; D000071837:Fibrillins; D005819:Genetic Markers; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism; D009687:Nuclear Proteins; D019696:Peptidylprolyl Isomerase; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D016601:RNA-Binding Proteins; D015854:Up-Regulation; D014746:Vimentin / Q000235:genetics / Q000378:metabolism; D019014:fas Receptor / Q000235:genetics / Q000378:metabolism; D054392:Adipokines
D048948:14-3-3 Proteins; D002352:Carrier Proteins; D018834:Chaperonin 60; D003300:Copper; D000091342:Endoplasmic Reticulum Chaperone BiP; D000071838:Fibrillin-1; D000071837:Fibrillins; D005819:Genetic Markers; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D008840:Microfilament Proteins; D009687:Nuclear Proteins; D019696:Peptidylprolyl Isomerase; D017346:Protein Serine-Threonine Kinases; D016601:RNA-Binding Proteins; D014746:Vimentin; D019014:fas Receptor; C578086:CWC22 protein, human; C000605722:FBN1 protein, human; D054392:Adipokines