Proteomic detection of prostate-specific antigen using a serum fractionation procedure: potential implication for new low-abundance cancer biomarkers detection

Solassol, Jérôme; Marin, Philippe; Demettre, Edith; Rouanet, Philippe; Bockaert, Joël; Maudelondé, Thierry; Mangé, Alain

doi:10.1016/j.ab.2004.11.031

Cited by 46 publications

(43 citation statements)

References 16 publications

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“…Fractionated serum, rather than whole serum, was used in this analysis because fractionation markedly increases the resolution and sensitivity of protein peak detection without any loss of minor proteins within the range of molecular weights detected using SELDI-TOF (Solassol et al, 2005;Mange et al, 2008). A total of 289 peaks were picked and clustered by the Biomarker Wizard software (Ciphergen, Fremount, CA, USA; see Excel files of absolute linear and normalized logtransformed intensity values of all serum in Supplementary Material Table S1).…”

Section: Resultsmentioning

confidence: 99%

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Serum protein signature may improve detection of ductal carcinoma in situ of the breast

et al. 2009

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Ductal carcinoma in situ (DCIS) of the breast is part of a spectrum of preinvasive lesions that originate within normal breast tissue and progress to invasive breast cancer. The detection of DCIS is important for the reduction of mortality from breast cancer, but the diagnosis of preinvasive breast tumors is hampered by the lack of an adequate detection method. To identify the changes in protein expression during the initial stage of tumorigenesis and to identify the presence of new DCIS markers, we analysed serum from 60 patients with breast cancer and 60 normal controls using mass spectrometry. A 23-protein index was generated that correctly distinguishes the DCIS and control groups with sensitivities and specificities in excess of 80% in two independent cohorts. Two candidate peptides were purified and identified as platelet factor 4 (PF-4) and complement C3a desArg anaphylatoxin (C3a desArg ) using liquid chromatography-tandem mass spectrometry (LC-MS/MS). In an independent serum set of 165 patients, PF-4 and C3a desArg were significantly upregulated in DCIS compared with non-cancerous controls, as validated using western blot and enzyme-linked immunosorbent assay. We conclude that our serum protein-based test, used in conjunction with image-based screening practices, could improve the sensitivity and specificity of breast cancer detection.

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Section: Resultsmentioning

confidence: 99%

“…To optimize the peak resolution and the number of protein peaks detected, an anion-exchange fractionation procedure was performed as described previously (Solassol et al, 2005). Each fraction was applied to a weak cation-exchange ProteinChip array surface (CM10).…”

Section: Proteomic Analysismentioning

confidence: 99%

Serum protein signature may improve detection of ductal carcinoma in situ of the breast

et al. 2009

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“…Previously, traditional 2-DE proteomic studies of PCa identified a large number of differentially expressed proteins and some were reported as potential markers for diagnosis of localized PCa (20)(21)(22)(23). Some studies of 2D-DIGE-based proteomics focused to identify novel clinically relevant proteins in PCa (24)(25)(26).…”

Section: Discussionmentioning

confidence: 99%

Quantitative proteomic study of human prostate cancer cells with different metastatic potentials

Wang

et al. 2016

International Journal of Oncology

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Abstract. Metastatic dissemination is a feature of most cancers including prostate cancer (PCa), and is the main cause of treatment failure and mortality. The aim of the study is to explore the mechanisms of PCa metastasis and to search for potential prognostic markers using proteomics. Two-dimensional fluorescent differential gel electrophoresis (2D-DIGE) was used to quantify proteins in normal prostate epithelial cells, bone metastasis-derived PC-3 cells, and visceral metastasis-derived PC-3M cells. Metastatic potential was confirmed by flow cytometry, electron microscopy, proliferating cell nuclear antigen assay, and wound healing assay. Differential protein expression was compared between PCa cells with different metastatic potentials (LNcap, DU145, PC-3 and PC-3M) and normal prostate epithelial cells (RWPE-1). Selected candidate proteins in human prostate tissues were analyzed using GOA, UniProt and GeneCards analyses. Eighty-six proteins were differentially expressed between cell lines (>1.5-fold, P<0.05). Among them, twelve proteins were identified by MALDI-TOF-MS. One protein was upregulated in normal prostate epithelial cells, nine proteins were upregulated in PC-3, and two proteins were upregulated in PC-3M. Proteins were divided into five groups according to their functions. The SETDB1 protein was closely associated with the prognosis of PCa. Bioinformatics suggested that SETDB1 might promote PCa bone metastasis through the WNT pathway. In conclusion, SETDB1 might be associated with the development of bone metastases from PCa. Further study is necessary to assess its exact role in PCa. IntroductionProstate cancer (PCa) is the most common malignancy in males and the second cause of cancer-related death in the USA and Europe (1). The incidence and mortality of PCa are rapidly increasing in China because of changes in diet and aging of the population (2). The proportion of PCa diagnosed at its early stage has increased because of the widespread screening of serum prostate-specific antigen (PSA) in the last two decades (3). However, many patients still present metastases at diagnosis, and metastases are the first factor leading to death from PCa (4). Patients with metastases do not benefit from radical prostatectomy or radiotherapy (5,6). Therefore, novel treatment approaches are needed.Proteomics is a powerful and effective tool to evaluate protein profiles (7). Two-dimensional fluorescent differential

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“…However, many glycoproteins with important biological functions are of low abundance, as above-mentioned CA125 and prostate-specific antigen [1][2][3][4]. When further treated with enzyme, the glycopeptides are only 2-5% in the digests.…”

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confidence: 99%

“…It could be seen that the numbers of such proteins identified in the insoluble fraction were obviously higher than that identified in the soluble fraction, especially for glycoproteins with the large number of TMDs. For example, the number of transmembrane glycoproteins with at least ten TMDs was increased by a factor of 14 (28/2), indicating that glycoproteins with relative high hydrophobicity could be efficiently identified from the insoluble fraction with the solubilization of BMIM BF 4 .…”

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confidence: 99%

Large‐scale N‐glycoproteome map of rat brain tissue: Simultaneous characterization of insoluble and soluble protein fractions

Qiao

Tao

et al. 2011

Proteomics

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The large-scale N-glycosylation analysis is critical for biomedical research, since a variety of diseases are found to be associated with glycoproteins. By a combination of glycoprotein analysis in insoluble protein fraction solubilized with 1% v/v 1-butyl-3-methylimidazolium tetrafluoroborate (BMIM BF 4 ) and those in soluble fraction, a total number of 462 nonredundant N-glycoprotein groups, including 316 transmembrane glycoproteins, were successfully identified. Correspondingly, 849 unique N-glycosites were confidently recognized. The data set could provide a support for the further in-depth research of brain N-glycosylation, such as for the discovery of candidate drug targets and biomarkers.

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Proteomic detection of prostate-specific antigen using a serum fractionation procedure: potential implication for new low-abundance cancer biomarkers detection

Cited by 46 publications

References 16 publications

Serum protein signature may improve detection of ductal carcinoma in situ of the breast

Serum protein signature may improve detection of ductal carcinoma in situ of the breast

Quantitative proteomic study of human prostate cancer cells with different metastatic potentials

Large‐scale N‐glycoproteome map of rat brain tissue: Simultaneous characterization of insoluble and soluble protein fractions

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