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Serum Peptidome Patterns of Colorectal Cancer Based on Magnetic Bead Separation and MALDI-TOF Mass Spectrometry Analysis

Institute of Anal-Colorectal Surgery, No. 150 Hospital of PLA, LuoYang 471000, China.
BioMed Research International (Impact Factor: 2.71). 10/2012; 2012:985020. DOI: 10.1155/2012/985020
Source: PubMed

ABSTRACT Background. Colorectal cancer (CRC) is one of the most common cancers in the world, identification of biomarkers for early detection of CRC represents a relevant target. The present study aims to determine serum peptidome patterns for CRC diagnosis.
Methods. The present work focused on serum proteomic analysis of 32 health volunteers and 38 CRC by ClinProt Kit combined with mass spectrometry. This approach allowed the construction of a peptide patterns able to differentiate the studied populations. An independent group of serum (including 33 health volunteers, 34 CRC, 16 colorectal adenoma, 36 esophageal carcinoma, and 31 gastric carcinoma samples) was used to verify the diagnostic and differential diagnostic capability of the peptidome patterns blindly. An immunoassay method was used to determine serum CEA of CRC and controls. Results. A quick classifier algorithm was used to construct the peptidome patterns for identification of CRC from controls. Two of the identified peaks at m/z 741 and 7772 were used to construct peptidome patterns, achieving an accuracy close to 100% (>CEA, P < 0.05). Furthermore, the peptidome patterns could differentiate validation group with high accuracy.
Conclusions. These results suggest that the ClinProt Kit combined with mass spectrometry yields significantly higher accuracy for the diagnosis and differential diagnosis of CRC.

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    • "Previously, an extensive proteomic analysis in the serum of patients with CRC was performed. A standardized serum preparation method for MALDI-TOF-MS was utilized based on WCX MB and was able to identify many valuable, low-abundance protein masses of interest [24]. However neither a characteristic protein cluster nor the structure identification of any of the proteins of the cluster was provided. "
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    ABSTRACT: Colorectal cancer (CRC) remains a major worldwide cause of cancer-related morbidity and mortality largely due to the insidious onset of the disease. The current clinical procedures utilized for disease diagnosis are invasive, unpleasant, and inconvenient. Hence, the need for simple blood tests that could be used for the early detection is crucial for its ultimate control and prevention. The present work is a case-control study focused on proteomic analysis of serum of healthy volunteers and CRC patients by the ClinProt profiling technology based on mass spectrometry. This approach allowed to identifying a pattern of proteins/peptides able to differentiate the studied populations. Moreover, some of peptides differentially expressed in the serum of patients as compared to healthy volunteers were identified by LTQ Orbitrap XL. A Quick Classifier Algorithm was used to construct the peptidome patterns (m/z 1208, 1467, 1505, 1618, 1656 and 4215) for the identification of CRC from healthy volunteers with accuracy close to 100% (>CEA, P < 0.05). Peaks at m/z 1505 and 1618 were identified as alpha-2-HS-glycoprotein precursor and tubulin beta chain, respectively. Alpha-2-HS-glycoprotein precursor and tubulin beta chain could be involved in the pathogenesis of CRC and perform as potential serology diagnosis biomarker.Virtual slides: The virtual slide(s) for this article can be found here: http://www.diagnosticpathology.diagnomx.eu/vs/4796578761089186.
    Diagnostic Pathology 03/2014; 9(1):53. DOI:10.1186/1746-1596-9-53 · 2.41 Impact Factor
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    • "). MALDI- TOF MS and MS can outcome peptides high throughput and sensitive investigation ClinProt (Bruker Daltonics, Ettlingen, Germany) which comprise a weak cationicexchanger magnetic beads-(WCX-MB) based sample separation, MALDI-TOF MS which collected peptide profiling, and created " disease-specific " peptidome pattern models, which can diagnose cancer for a powerful tool (Maurer et al., 2011; Fan et al., 2012). Many studies have shown that low molecular weight region, particularly peptides smaller than 20 kD, which may provide a novel means of diagnosing cancer and other diseases (Dai et al., 2010; Liu et al., 2010; Sui et al., 2010). "
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    ABSTRACT: Esophageal cancer (EC) is one of the most common malignant tumors, and the incidence of esophageal squamous cell carcinoma (ESCC) is highest in China. Early diagnosis and effective monitoring are keys to comprehensive treatment and discovering tumor metastases and recurrence in time. The aim of this study was to confirm serum peptidome pattern utility for diagnosis of ESCC, and assessment of operation success, postoperative chemotherapy results, tumor metastasis and recurrence. Serum samples were collected from 61 patients treated with surgery and chemotherapy and 20 healthy individuals. Spectral data generated with weak cationic-exchanger magnetic beads (WCX-MB) and MALDI-TOF MS by a support vector machine (SVM), were used to construct diagnostic models and system training as potential biomarkers. A pattern consisting of 11 protein peaks, separated ESCC (m/z 650.75), operated (m/z 676.61, 786.1, 786.58), postoperative chemotherapy (m/z 622.77, 650.66, 676.46) and tumor metastasis and recurrence (m/z 622.63, 650.56, 690.77, 676.12) from the healthy individuals with a sensitivity of 100.0% and a specificity of 100.0%. These results suggested that MALDI- TOF MS combined with MB separation yields significantly higher sensitivity and specificity for the detection of serum protein in patients with EC patients treated with surgery and chemotherapy.
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    ABSTRACT: OBJECTIVE: Despite major advances in its diagnosis and treatment, gastric cancer (GC) remains a major life-threatening disease. Treatment of the disease is further aggravated by the lack of diagnostic biomarkers that can aid in the early detection of GC and promote its favorable prognosis. The present work aims to identify novel diagnostic biomarkers for GC. DESIGN AND METHODS: The present work is a case-control study that focuses on proteomic analysis of serum from healthy volunteers and GC patients using ClinProt profiling technology based on mass spectrometry. A pattern of proteins/peptides with the ability to differentiate the studied populations was identified. Deregulated proteins/peptides differentially expressed in the serum of patients compared with healthy volunteers were identified by mass spectroscopy. RESULTS: A pattern of proteins/peptides consisting of four protein/peptide peaks at m/z 1467, 1867, 2701, and 2094 was identified. These protein/peptide peaks were able to differentiate the studied populations with close to 100% sensitivity and specificity. Three of the deregulated proteins/peptides at m/z 1867, 2701, and 2094 were identified by mass spectroscopy (LTQ Orbitrap XL) as tubulin beta chain, thymosin beta-4-like protein 3, and cytochrome b-c1 complex subunit 1, respectively. CONCLUSIONS: The pattern of proteins/peptides identified in the present work shows great potential for GC diagnosis. Deregulated proteins of tubulin beta chain, thymosin beta-4-like protein 3, and cytochrome b-c1 complex subunit 1 may be involved in the pathogenesis of GC and serve as potential serological diagnostic biomarkers.
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