Secretome proteomics for discovery of cancer biomarkers

Makridakis, Manousos; Vlahou, Antonia

doi:10.1016/j.jprot.2010.07.001

Cited by 231 publications

(212 citation statements)

References 103 publications

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“…In addition, extracellular matrix components and other molecules secreted by tumor cells are rich sources of potential markers and drug targets for cancer treatment (Makridakis et al, 2010). The study found that DHA promoted the cell secretions of TCTP protein in the cell culture supernatant.…”

Section: Discussionmentioning

confidence: 92%

Targeted Efficacy of Dihydroartemisinin for Translationally Controlled Protein Expression in a Lung Cancer Model

Liu

Wu²,

Guo³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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Objective: Lung cancer is one of the malignant tumors with greatest morbidity and mortality around the world. The keys to targeted therapy are discovery of lung cancer biomarkers to facilitate improvement of survival and quality of life for the patients with lung cancer. Translationally controlled tumor protein (TCTP) is one of the most overexpressed proteins in human lung cancer cells by comparison to the normal cells, suggesting that it might be a good biomarker for lung cancer. Materials and Methods: In the present study, the targeted efficacy of dihydroartemisinin (DHA) on TCTP expression in the A549 lung cancer cell model was explored. Results and Conclusions: DHA could inhibit A549 lung cancer cell proliferation, and simultaneously up-regulate the expression of TCTP mRNA, but down-regulate its protein expression in A549 cells. In addition, it promoted TCTP protein secretion. Therefore, TCTP might be used as a potential biomarker and therapeutic target for non-small cell lung cancers.

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Section: Discussionmentioning

confidence: 92%

Targeted Efficacy of Dihydroartemisinin for Translationally Controlled Protein Expression in a Lung Cancer Model

Liu

Wu²,

Guo³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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“…These proteins are released by the classical secretion mechanism or are shed from the cell surface. Because of cell lysis and other non-classical secretion mechanisms, some intracellular proteins, such as actin, carbonyl reductase and glyceraldehyde-3-phosphate dehydrogenase, were present in the CM [8]. In addition, 217 differential proteins, such as the liver form of glycogen phosphorylase, may participate in specific HCC-related processes ( Figure S1B).…”

Section: Discussionmentioning

confidence: 99%

“…Because of the formidable challenges of direct analysis of plasma/ serum samples, the secretome has been pursued as an alternative approach for blood biomarker discovery. Secreted proteins are also most likely excellent candidate serological tumor markers because they are released by cells and thus have the highest potential to enter the circulation [8]. For example, Planque et al [9] identified five biomarker candidates in plasma by analyzing conditioned media (CM) from four lung cancer cell lines.…”

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confidence: 99%

Secretory/releasing proteome-based identification of plasma biomarkers in HBV-associated hepatocellular carcinoma

Yang

Rong

Xiao

et al. 2013

Sci. China Life Sci.

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For successful therapy, hepatocellular carcinoma (HCC) must be detected at an early stage. Herein, we used a proteomic approach to analyze the secretory/releasing proteome of HCC tissues to identify plasma biomarkers. Serum-free conditioned media (CM) were collected from primary cultures of cancerous tissues and surrounding noncancerous tissues. Proteomic analysis of the CM proteins permitted the identification of 1365 proteins. The enriched molecular functions and biological processes of the CM proteins, such as hydrolase activity and catabolic processes, were consistent with the liver being the most important metabolic organ. Moreover, 19% of the proteins were characterized as extracellular or membrane-bound. For validation, secretory proteins involved in transforming growth factor-β signaling pathways were validated in plasma samples. Alphafetoprotein (AFP), metalloproteinase (MMP)1, osteopontin (OPN), and pregnancy-specific beta-1-glycoprotein (PSG)9 were significantly increased in HCC patients. The overall performance of MMP1 and OPN in the diagnosis of HCC remained greater than that of AFP. In addition, this study represents the first report of MMP1 as a biomarker with a higher sensitivity and specificity than AFP. Thus, this study provides a valuable resource of the HCC secretome with the potential to investigate serological biomarkers. MMP1 and OPN could be used as novel biomarkers for the early detection of HCC and to improve the sensitivity of biomarkers compared with AFP. hepatocellular carcinoma (HCC), secretome, biomarker, MMP1, OPN, PSG9 Citation:Yang L, Rong W Q, Xiao T, et al. Secretory/releasing proteome-based identification of plasma biomarkers in HBV-associated hepatocellular carcinoma. Sci China Life Sci, 2013Sci, , 56: 638-646, doi: 10.1007 Approximately 600000 new cases of hepatocellular carcinoma (HCC) are diagnosed each year, of which approximately 55% are detected in China [1]. The relationship between HCC and persistent hepatitis B virus (HBV) infection has been well documented. More than 20 million individuals suffer from chronic HBV infection in China [2]. Surgical resection is the most effective treatment for HCC patients, but the reported five-year disease-free survival rate is only

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“…Analyses of the complete set of secreted proteins -otherwise known as the "secretome" -have been reported in various organisms, cell types, and pathologies, and are quickly gaining popularity [6,7]. Not surprisingly, several studies have focused on analyses of cancer-or metastasis-specific changes in secretome profiles [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Global secretome analysis identifies novel mediators of bone metastasis

et al. 2012

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Bone is the one of the most common sites of distant metastasis of solid tumors. Secreted proteins are known to influence pathological interactions between metastatic cancer cells and the bone stroma. To comprehensively profile secreted proteins associated with bone metastasis, we used quantitative and non-quantitative mass spectrometry to globally analyze the secretomes of nine cell lines of varying bone metastatic ability from multiple species and cancer types. By comparing the secretomes of parental cells and their bone metastatic derivatives, we identified the secreted proteins that were uniquely associated with bone metastasis in these cell lines. We then incorporated bioinformatic analyses of large clinical metastasis datasets to obtain a list of candidate novel bone metastasis proteins of several functional classes that were strongly associated with both clinical and experimental bone metastasis. Functional validation of selected proteins indicated that in vivo bone metastasis can be promoted by high expression of (1) the salivary cystatins CST1, CST2, and CST4; (2) the plasminogen activators PLAT and PLAU; or (3) the collagen functionality proteins PLOD2 and COL6A1. Overall, our study has uncovered several new secreted mediators of bone metastasis and therefore demonstrated that secretome analysis is a powerful method for identification of novel biomarkers and candidate therapeutic targets.

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Secretome proteomics for discovery of cancer biomarkers

Cited by 231 publications

References 103 publications

Targeted Efficacy of Dihydroartemisinin for Translationally Controlled Protein Expression in a Lung Cancer Model

Targeted Efficacy of Dihydroartemisinin for Translationally Controlled Protein Expression in a Lung Cancer Model

Secretory/releasing proteome-based identification of plasma biomarkers in HBV-associated hepatocellular carcinoma

Global secretome analysis identifies novel mediators of bone metastasis

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