TY - JOUR
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: dsul@korea.ac.kr
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.
UR - http://www.scopus.com/inward/record.url?scp=77958171659&partnerID=8YFLogxK
U2 - 10.1080/15287394.2010.511583
DO - 10.1080/15287394.2010.511583
M3 - Article
C2 - 20954082
AN - SCOPUS:77958171659
SN - 1528-7394
VL - 73
SP - 1570
EP - 1585
JO - Journal of Toxicology and Environmental Health - Part A: Current Issues
JF - Journal of Toxicology and Environmental Health - Part A: Current Issues
IS - 21-22
ER -