Proteomic analysis of proteins secreted by HepG2 cells treated with butyl benzyl phthalate

Seonyoung Choi; So Young Park; Dongsub Kwak; Sohee Phark; Min Lee; Ji Youn Lim; Woon Won Jung; Donggeun Sul

doi:10.1080/15287394.2010.511583

Proteomic analysis of proteins secreted by HepG2 cells treated with butyl benzyl phthalate

Seonyoung Choi, So Young Park, Dongsub Kwak, Sohee Phark, Min Lee, Ji Youn Lim, Woon Won Jung, Donggeun Sul

Department of Medicine

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

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 μM) 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.

Original language	English
Pages (from-to)	1570-1585
Number of pages	16
Journal	Journal of Toxicology and Environmental Health - Part A: Current Issues
Volume	73
Issue number	21-22
DOIs	https://doi.org/10.1080/15287394.2010.511583
Publication status	Published - 2010

Bibliographical note

Funding Information:
Seonyoung Choi1,∗, So-Young Park, and Donggeun Sul contributed equally to this work and are considered as co-first author. This work was supported by the Ministry of Environment as “The Eco-Technopia 21 project” (number 2009-09001-0075-0) and by the ACE program through the National Research Foundation of Korea (NRF) grant funded by the Korean Ministry of Education, Science, and Technology (MEST) (number 2009-009-1414). Address correspondence to Donggeun Sul, PhD, Graduate School of Medicine, Korea University, 126-1, Anam-dong 5-ga, Seongbuk-gu, Seoul 136-701, Korea. E-mail: [email protected]

ASJC Scopus subject areas

Toxicology
Health, Toxicology and Mutagenesis

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10.1080/15287394.2010.511583

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title = "Proteomic analysis of proteins secreted by HepG2 cells treated with butyl benzyl phthalate",

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 μM) 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.",

author = "Seonyoung Choi and Park, {So Young} and Dongsub Kwak and Sohee Phark and Min Lee and Lim, {Ji Youn} and Jung, {Woon Won} and Donggeun Sul",

note = "Funding Information: Seonyoung Choi1,∗, So-Young Park, and Donggeun Sul contributed equally to this work and are considered as co-first author. This work was supported by the Ministry of Environment as “The Eco-Technopia 21 project” (number 2009-09001-0075-0) and by the ACE program through the National Research Foundation of Korea (NRF) grant funded by the Korean Ministry of Education, Science, and Technology (MEST) (number 2009-009-1414). Address correspondence to Donggeun Sul, PhD, Graduate School of Medicine, Korea University, 126-1, Anam-dong 5-ga, Seongbuk-gu, Seoul 136-701, Korea. E-mail: [email protected]",

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T1 - Proteomic analysis of proteins secreted by HepG2 cells treated with butyl benzyl phthalate

AU - Choi, Seonyoung

AU - Park, So Young

AU - Kwak, Dongsub

AU - Phark, Sohee

AU - Lee, Min

AU - Lim, Ji Youn

AU - Jung, Woon Won

AU - Sul, Donggeun

N1 - Funding Information: Seonyoung Choi1,∗, So-Young Park, and Donggeun Sul contributed equally to this work and are considered as co-first author. This work was supported by the Ministry of Environment as “The Eco-Technopia 21 project” (number 2009-09001-0075-0) and by the ACE program through the National Research Foundation of Korea (NRF) grant funded by the Korean Ministry of Education, Science, and Technology (MEST) (number 2009-009-1414). Address correspondence to Donggeun Sul, PhD, Graduate School of Medicine, Korea University, 126-1, Anam-dong 5-ga, Seongbuk-gu, Seoul 136-701, Korea. E-mail: [email protected]

PY - 2010

Y1 - 2010

N2 - 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 μM) 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.

AB - 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 μM) 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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ER -

Proteomic analysis of proteins secreted by HepG2 cells treated with butyl benzyl phthalate

Abstract

Bibliographical note

ASJC Scopus subject areas

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