Analysis of post-operative changes in serum protein expression profiles from colorectal cancer patients by MALDI-TOF mass spectrometry: a pilot methodological study

Liao, Christopher C L; Mehta, Anuja; Ward, Nicholas J; Marsh, Simon; Arulampalam, Tan; Norton, John D.

doi:10.1186/1477-7819-8-33

Cited by 13 publications

(7 citation statements)

References 34 publications

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“…MALDI-TOF-MS is capable of detecting proteins that can aid in the diagnosis of many common types of cancer. Serum proteomics profiling may also help predict the response to treatment, in addition to improving our understanding of metastasis (18). Such analyses have identified several clues concerning the markers of metastasis.…”

Section: Discussionmentioning

confidence: 99%

Comparative serum proteomic analysis involving liver organ-specific metastasis-associated proteins of nasopharyngeal carcinoma

Pan

Tao

Zhao

et al. 2012

Experimental and Therapeutic Medicine

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Metastasis is the main cause of cancer-related mortality; patients with liver metastases (LM) have the worst prognosis among patients with nasopharyngeal carcinoma (NPC). However, at present, few biomarkers for detecting organ-specific metastasis have been identified. Proteomics, an ultra-sensitive analytical technique, can detect molecular changes before organ-specific metastasis occurs. Analysis with matrix-assisted, laser desorption-ionization time-of-flight mass spectrometry (MALDI-TOF-MS), combined with magnetic chemical affinity beads is a new technique for evaluating protein separation. We sought to identify potential liver-specific, metastasis-associated proteomic printing in patients with NPC. We examined 64 serum samples from 50 patients who had pathologically confirmed NPC and 14 who had pathologically confirmed non-NPC with LM using MALDI-TOF-MS with weak cation bead protein chips. During follow-up of at least 37 months (maximum, 176 months) following radiotherapy, we confirmed 16 cases of LM (LM NPC), 16 cases without LM (non-LM NPC) and 18 cases without metastasis (non-M NPC). Using comparison analysis, 4 protein mass peaks, 4155.34, 4194.87, 4210.78 and 4249.56 m/z were identified as liver-specific, metastasis-associated protein peaks in NPC and two of them (4155 and 4249 m/z) met two different statistical criteria in both ClinProt software analyses and discriminant analyses. Models based on the 4 potential serum markers of NPC discriminated between LM NPC, non-LM NPC, non-M NPC and non-NPC LM analyzed with sieved markers. The recognition capability and cross-validation of these models for differentiating the above 4 groups are all approximately 80%. MALDI-TOF-MS combined with tree analysis models may provide a clinical diagnostic platform for detecting potential liver-specific, metastasis-associated proteomic printing in NPC. However, markedly differential proteins still need to be identified.

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Section: Discussionmentioning

confidence: 99%

Comparative serum proteomic analysis involving liver organ-specific metastasis-associated proteins of nasopharyngeal carcinoma

Pan

Tao

Zhao

et al. 2012

Experimental and Therapeutic Medicine

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“…There are several studies published where MALDI/SELDI-based analyses of the low-molecular-weight fraction of serum/plasma proteome were applied for identification of peptide signatures specific for patients with head and neck cancer (30)(31)(32)(33)(34), colorectal cancer (19,(35)(36)(37)(38) and lung cancer (39)(40)(41)(42)(43)(44). All these works proposed differentiating peptides and multi-peptide signatures that discriminated between specimens collected from cancer patients and healthy donors, yet such cancer signatures were built of apparently different spectral components.…”

Section: Discussionmentioning

confidence: 99%

Comparison of peptide cancer signatures identified by mass spectrometry in serum of patients with head and neck, lung and colorectal cancers: Association with tumor progression

Pietrowska

Polańska²,

Suwiński³

et al. 2011

Int J Oncol

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Abstract. Mass spectrometry-based analyses of the lowmolecular-weight fraction of serum proteome allow identifying proteome profiles (signatures) that are potentially useful in detection and diagnostics of cancer. Here we compared serum proteome profiles of healthy donors and patients with three different types of cancer aiming to identify peptide signatures that were either common for all cancer samples or specific for cancer type. Blood samples were collected before start of the therapy from patients with head and neck squamous cell cancer, colorectal adenocarcinoma and non-small cell lung cancer, and from a corresponding group of healthy volunteers. Mass profiles of the serum proteome were recorded in the range between 2 and 13 kDa using MALDI-ToF spectrometry and 131 identified peptide ions were used for statistical analyses. Similar degrees of overall similarities were observed in all intra-group and inter-group analyses when general features of serum proteome profiles were compared between individual samples. However, classifiers built of selected spectral components allowed differentiation between healthy donors and three groups of cancer patients with 69-74% sensitivity and 82-84% specificity. There were two common peptide species (3766 and 5867 Da) with increased levels in all cancer samples. Several spectral components permitted differentiation between lung cancer samples and either head and neck cancer or colorectal cancer samples, but two latter types of samples could not be properly discriminated. Abundance of spectral components that putatively corresponded to fragments of serum amyloid A (11511 and 11667 Da) was highest in lung cancer samples, yet increased levels of these peptides appeared to generally associate with more advanced cancer cases. We concluded that certain components of serum peptide signatures are common for different cancer signatures and putatively reflect general response of organism to the disease, yet other components of such signatures are more specific and most likely correspond to clinical stage of the malignancy. IntroductionThe low-molecular-weight fraction of the blood proteome appears to be a promising source of novel biomarkers of human diseases. Thus, mass spectrometry (MS) methods, which allow characterization of this particular component of human proteome, emerge as a valuable tool of clinical proteomics and disease diagnostics (1-5). The proteomics approach that takes into consideration characteristic features of the whole proteome but does not rely on particular protein, is called proteome pattern analysis or proteome profiling. In this approach specific proteome signatures are built based on several peptide/protein components, which can be exemplified by ions registered at defined m/z values in the mass spectrum. Such signatures can be used for sample identification and classification even though their particular components may lack differentiating power when analyzed separately (6-9). Matrix-assisted laser desorption/ionization spectrometry (MALDI), and its deri...

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“…Vimentin was identified as promoter of tumor cell invasiveness. Liao and co-workers identified diagnostic peptidome signatures from sera from patients with colorectal cancer [62]. Although this was a pilot study, the methodology used could be relevant in clinical evaluation of disease recurrence.…”

Section: Mass Spectrometrymentioning

confidence: 99%

Proteomic strategies and challenges in tumor metastasis research

Hudler

Gorsic

Komel

2010

Clin Exp Metastasis

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The rapidly evolving field of proteomics offers new approaches to understanding the pathogenesis of cancer and metastatic disease. Although numerous tumor markers have been identified with different genomic methods in the past, most are either not specific or sensitive enough to be used in routine clinical setting. The rationale for proteomic profiling is based on the fact that proteins represent the dynamic state of the cells, reflecting pathophysiological changes in the disease more accurately than genomic and epigenetic alterations. Emerging proteomic techniques allow simultaneous assessment of a large number of proteins at one time. The study of protein profiles in complex systems, such as plasma, serum or tissues of cancer patients is likely to become valuable for monitoring the response of patients during treatment or for detecting recurrence of the disease.

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Analysis of post-operative changes in serum protein expression profiles from colorectal cancer patients by MALDI-TOF mass spectrometry: a pilot methodological study

Cited by 13 publications

References 34 publications

Comparative serum proteomic analysis involving liver organ-specific metastasis-associated proteins of nasopharyngeal carcinoma

Comparative serum proteomic analysis involving liver organ-specific metastasis-associated proteins of nasopharyngeal carcinoma

Comparison of peptide cancer signatures identified by mass spectrometry in serum of patients with head and neck, lung and colorectal cancers: Association with tumor progression

Proteomic strategies and challenges in tumor metastasis research

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