Targeted quantitative analysis of superoxide dismutase 1 in cisplatin-sensitive and cisplatin-resistant human ovarian cancer cells
| Autor: | Heather Sahm, Tony J. Tegeler, Bei Nie, Jong Won Kim, Jin Sam You, Mu Wang, Dawn P. G. Brown |
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| Rok vydání: | 2010 |
| Předmět: |
Proteomics
Clinical Biochemistry Quantitative proteomics SOD1 Peptide Sensitivity and Specificity Biochemistry Mass Spectrometry Article Analytical Chemistry Superoxide Dismutase-1 Cell Line Tumor Enzyme Stability medicine Humans Ovarian Neoplasms Cisplatin chemistry.chemical_classification Superoxide Dismutase Chemistry Selected reaction monitoring Reproducibility of Results Cell Biology General Medicine medicine.disease Molecular biology Peptide Fragments Drug Resistance Neoplasm Female Ovarian cancer Quantitative analysis (chemistry) medicine.drug |
| Zdroj: | Journal of Chromatography B. 878:700-704 |
| ISSN: | 1570-0232 |
| Popis: | Protein quantification in a complex protein mixture presents a daunting task in biochemical analysis. Antibody-based immunoassays are traditional methods for protein quantification. However, there are issues associated with accuracy and specificity in these assays, especially when the changes are small (e.g., < 2-fold). With recent developments in mass spectrometry, monitoring a selected peptide, thus protein, in a complex biological sample has become possible. In this study, we demonstrate a simple mass spectrometry-based method for selective measurement of a moderately low abundant protein, superoxide dismutase 1 (SOD1), in cisplatin-sensitive and cisplatin-resistant human ovarian cancer cells. Selected-reaction-monitoring (SRM) technology was employed to specifically analyze the target peptides in a pair of human ovarian cancer cell lines: 2008/2008-C13*5.25 (cisplatin-sensitive/cisplatin-resistant, respectively). The observed 1.47 fold higher expression in the resistant cell line is consistent with findings by other approaches. This robust liquid chromatography/mass spectrometry (LC/MS) method provides a powerful tool for targeted proteomic verification and/or validation studies. |
| Databáze: | OpenAIRE |
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