Colorectal cancer candidate biomarkers identified by tissue secretome proteome profiling

Wit, Meike de; Kant, Huub; Piersma, Sander R.; Pham, Thang V.; Mongera, Sandra; Berkel, Maaike P.A. van; Boven, Epie; Pontén, Fredrik; Meijer, Gerrit A.; Jiménez, Connie R.; Fijneman, Remond J.A.

doi:10.1016/j.jprot.2014.01.001

Cited by 85 publications

(60 citation statements)

References 48 publications

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“…As a secreted glycoprotein, OLFM4 is an obvious candidate biomarker. Mass spectrometry used to analyse cellular proteomes including secretomes, identified OLFM4 as a candidate biomarker in colorectal cancer 21, 22. In accordance, a Japanese study found significantly higher plasma levels of OLFM4 in 123 gastric cancer patients compared to healthy controls 23.…”

Section: Introductionmentioning

confidence: 73%

Plasma levels of OLFM4 in normals and patients with gastrointestinal cancer

Clemmensen

Glenthøj

Heebøll

et al. 2015

J Cellular Molecular Medi

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Olfactomedin 4 (OLFM4) is a secreted glycoprotein predominantly expressed in bone marrow and gastrointestinal tissues. Aberrant expression of OLFM4 has been shown in several cancers. However, the clinical significance hereof is currently controversial. OLFM4 has been proposed as a candidate biomarker of gastrointestinal cancers. To address this, we developed monoclonal antibodies against synthetic peptides representing various segments of OLFM4. We examined expression of OLFM4 in epithelial cells by immunohistochemistry and found that OLFM4 is highly expressed in proliferating benign epithelial cells and in some carcinoma cells. We developed an Enzyme Linked Immunosorbent Assay for OLFM4 and investigated whether plasma levels of OLFM4 reflect colorectal malignancies, but were unable to see any such association. Instead, we observed two populations of individuals with respect to OLFM4 levels in plasma, the majority with OLFM4 in plasma between 0 and 0.1 μg/ml, mean 0.028 μg/ml while 10% of both normals and patients with cancers had OLFM4 between 4 and 60 μg/ml, mean 15 μg/ml. The levels were constant over time. The background for this high plasma level is not known, but must be taken into account if OLFM4 is used as biomarker for GI cancers.

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Section: Introductionmentioning

confidence: 73%

Plasma levels of OLFM4 in normals and patients with gastrointestinal cancer

Clemmensen

Glenthøj

Heebøll

et al. 2015

J Cellular Molecular Medi

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“…Proteins with signal peptides are usually secreted through conventional pathways involving the endoplasmic reticulum-Golgi system. Unconventional secretory pathways include (1) translocation across the plasma membrane, (2) lysosome-dependent pathways, and (3) extracellular vesicles-dependent secretion (74). We examined probable secretion pathways for the 23 candidate proteins.…”

Section: Figmentioning

confidence: 99%

Targeted Proteomics for Multiplexed Verification of Markers of Colorectal Tumorigenesis

Uzozie

Selevsek

Wåhlander

et al. 2017

Molecular & Cellular Proteomics

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Targeted proteomic methods can accelerate the verification of multiple tumor marker candidates in large series of patient samples. We utilized the targeted approach known as selected/multiple reaction monitoring (S/MRM) to verify potential protein markers of colorectal adenoma identified by our group in previous transcriptomic and quantitative shotgun proteomic studies of a large cohort of precancerous colorectal lesions. We developed SRM assays to reproducibly detect and quantify 25 (62.5%) of the 40 selected proteins in an independent series of precancerous and cancerous tissue samples (19 adenoma/ normal mucosa pairs; 17 adenocarcinoma/normal mucosa pairs). Twenty-three proteins were significantly upregulated (n ‫؍‬ 17) or downregulated (n ‫؍‬ 6) in adenomas and/or adenocarcinomas, as compared with normal mucosa (linear fold changes > ؎1.3, adjusted p value <0.05). Most changes were observed in both tumor types (up-regulation of ANP32A, ANXA3, SORD, LDHA, LCN2, NCL, S100A11, SERPINB5, CDV3, OLFM4, and REG4; downregulation of ARF6 and PGM5), and a fiveprotein biomarker signature distinguished neoplastic tissue from normal mucosa with a maximum area under the receiver operating curve greater than 0.83. Other changes were specific for adenomas (PPA1 and PPA2 up-regulation; KCTD12 downregulation) or adenocarcinoma (ANP32B, G6PD, RCN1, and SET up-regulation; downregulated AKR1B1, APEX1, and PPA1). Some changes significantly correlated with a few patient-or tumor-related phenotypes. Twenty-two (96%) of the 23 proteins have a potential to be released from the tumors into the bloodstream, and their detectability in plasma has been previously reported. The proteins identified in this study expand the pool of biomarker candidates that can be used to develop a standardized precolonoscopy blood test for the early detection of colorectal tumors. Molecular & Cellular

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“…Fisher's exact test was used to account for the sample pairing using the protein analysis program Scaffold Q+ version 4.4.3. A fold-change cut-off of 1.5 and a P-value cut-off of 0.05, as used by various quantitative proteomic studies (19)(20)(21)(22), were used as minimum criteria for differential protein expression. The construction of the interaction pathways between the differentially-expressed proteins was generated by Integrated System Interactome (24).…”

Section: Analysis Of Dius By Nano-lc-quadrupole-time-of-flight (Nlc-qmentioning

confidence: 99%

Proteomic profile of saliva and plasma from women with impalpable breast lesions

et al. 2016

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Abstract. The present study evaluated the proteomic profile of saliva and plasma from women with impalpable breast lesions using nano-liquid chromatography-quadrupole-time-of-flight (nLC-Q-TOF) technology. Plasma and saliva from patients with fibroadenoma (n=10), infiltrating ductal carcinoma (n=10) and healthy control groups (n=8) were assessed by combinations of inter/intra-group analyses, revealing significant quantitative and qualitative differences. The major differentially-expressed proteins in the saliva of patients compared with the controls were α2-macroglobulin and ceruloplasmin, but the proteins that met the minimum fold-change and P-value cut-offs were leukocyte elastase inhibitor and α-enolase, and deleted in malignant brain tumors 1. Concerning plasma, α-2-macroglobulin and ceruplasmin were upregulated, while other proteins such as haptoglobin, hemopexin and vitamin D-binding protein were downregulated compared with the control. The changes in immune, molecular transport and signaling pathways were the most representative in the proteomic profile of the saliva and plasma. This is the first study to describe the proteome of saliva and plasma from the same women with impalpable breast lesions.

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Colorectal cancer candidate biomarkers identified by tissue secretome proteome profiling

Cited by 85 publications

References 48 publications

Plasma levels of OLFM4 in normals and patients with gastrointestinal cancer

Plasma levels of OLFM4 in normals and patients with gastrointestinal cancer

Targeted Proteomics for Multiplexed Verification of Markers of Colorectal Tumorigenesis

Proteomic profile of saliva and plasma from women with impalpable breast lesions

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