Proteomic Analysis of Proteins Secreted by HepG2 Cells Treated with Butyl Benzyl Phthalate
| Autor: | Min Lee, Sohee Phark, Ji Youn Lim, Seonyoung Choi, Dongsub Kwak, So Young Park, Woon Won Jung, Donggeun Sul |
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| Rok vydání: | 2010 |
| Předmět: |
Male
Proteomics Silver Staining Spectrometry Mass Electrospray Ionization Proteome Cell Survival Health Toxicology and Mutagenesis Protein subunit Blotting Western Phthalic Acids Tetrazolium Salts Toxicology Tandem mass spectrometry Peptide Mapping Rats Sprague-Dawley chemistry.chemical_compound Western blot Tandem Mass Spectrometry Biomarkers Tumor medicine Animals Humans Electrophoresis Gel Two-Dimensional Gel electrophoresis Formazans medicine.diagnostic_test Liver Neoplasms Phthalate Hep G2 Cells Microarray Analysis Molecular biology Rats Blot Teratogens chemistry Biochemistry Comet Assay Isoelectric Focusing Gelsolin DNA Damage |
| Zdroj: | Journal of Toxicology and Environmental Health, Part A. 73:1570-1585 |
| ISSN: | 1087-2620 1528-7394 |
| DOI: | 10.1080/15287394.2010.511583 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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