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Proteomic Analysis of Proteins Secreted by HepG2 Cells Treated with Butyl Benzyl Phthalate

Authors
Choi, SeonyoungPark, So-YoungKwak, DongsubPhark, SoheeLee, MinLim, Ji-YounJung, Woon-WonSul, Donggeun
Issue Date
2010
Publisher
TAYLOR & FRANCIS INC
Citation
JOURNAL OF TOXICOLOGY AND ENVIRONMENTAL HEALTH-PART A-CURRENT ISSUES, v.73, no.21-22, pp.1570 - 1585
Indexed
SCIE
SCOPUS
Journal Title
JOURNAL OF TOXICOLOGY AND ENVIRONMENTAL HEALTH-PART A-CURRENT ISSUES
Volume
73
Number
21-22
Start Page
1570
End Page
1585
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/118527
DOI
10.1080/15287394.2010.511583
ISSN
1528-7394
Abstract
Proteomic changes in proteins secreted by human hepatocellular carcinomas (HepG2) cells exposed to butyl benzyl phthalate (BBP) were evaluated. HepG2 cells were treated with three different concentrations of BBP (0, 10, or 25 M) for 24 or 48 h. Following incubation, the cells were subjected to proteomic analysis using two different pI ranges (4-7 and 6-9) and large-size two-dimensional gel electrophoresis. Results showed resolution of a total of 2776 protein spots. Of these, 29, including 19 upregulated and 10 downregulated proteins, were identified by electrospray ionization-mass spectrometry-mass spectrometry (ESI-MS/MS). Among these, the identities of cystatin C, Rho guanine nucleotide dissociation inhibitor, gelsolin, DEK protein, Raf kinase inhibitory protein, triose phosphate isomerase, heptaglobin-related protein, inter-alpha-trypsin inhibitor heavy chain H2, and electron transfer flavoprotein subunit beta were confirmed by Western blot analysis. These proteins were found to be involved in apoptosis, signaling, tumor progression, energy metabolism, and cell structure and motility. Therefore, these proteins have potential to be employed as biomarkers of BBP exposure and may be useful in understanding mechanisms underlying the adverse effects of BBP.
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