Differential signatures of protein glycosylation and phosphorylation in human Chang liver cells induced by TCDD treatment = TCDD 처리에 의한 인간 Chang 세포의 당화와 인산화 변화패턴 연구
Cited 12 time in
- Differential signatures of protein glycosylation and phosphorylation in human Chang liver cells induced by TCDD treatment = TCDD 처리에 의한 인간 Chang 세포의 당화와 인산화 변화패턴 연구
- Ji Hye Kim; Y J In; Won Kon-Kim; Kwang-Hee Bae; Sunghyun Kang; Sang Chul Lee
- Bibliographic Citation
- Toxicology Letters, vol. 178, no. 1, pp. 20-28
- Publication Year
- Dioxins are a class of polyhalogenated aromatic hydrocarbons that induces a wide spectrum of toxic responses in animals. Health effects have been studied intensively, but the detailed molecular mechanisms are quite complex and not yet fully understood. In this study, the effects of model dioxin, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on protein modifications such as glycosylation and phosphorylation were extensively studied. Using 2-D electrophoresis, various protein visualizations techniques, protein modification-dependent enrichments techniques and mass spectrometry, we performed comparative proteomic investigations on Chang human liver cells before and after the treatment with TCDD. Many glycoproteins and phosphoproteins were found to be affected by the TCDD treatment. The glycosylations on Cathepsin B, HSP60, the subunit 5 of chaperonin containing TCP1 complex, and Prolyl 4-hydroxylase β-subunit were increased. Heat shock 70 kDa protein 5 and ATP synthase β subunit showed enhanced or reduced phosphorylation, respectively. Two microtubule associated proteins, Microtubule-associated protein 1S and ARP1 actin-related protein 1 homolog A showed enhanced tyrosine phosphorylation. The data in this study provide interesting insights on the molecular and biochemical events of TCDD-mediated toxicities.
- Dioxin; Glycosylation; Liver; Phosphorylation; Proteomics
- Appears in Collections:
- Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
- Files in This Item:
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.