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Title 

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

Authors 

Ji Hye KimY J InWon Kon KimKwang-Hee BaeSunghyun KangSang Chul Lee

Publisher 

Elsevier

Issue Date 

2008

Citation 

Toxicology Letters, vol. 178, no. 1, pp. 20-28

Keywords 

dioxinglycosylationliverphosphorylationproteomicsactin related proteinglycoproteinheat shock protein 60heat shock protein 70microtubule associated protein

Abstract 

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.

ISSN 

0378-4274

Link 

http://dx.doi.org/10.1016/j.toxlet.2008.01.019

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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