Glycoproteomics using fluid‐based specimens in the discovery of lung cancer protein biomarkers: Promise and challenge

Li, Qing Kay; Gabrielson, Edward; Askin, Frederic B.; Chan, Daniel W.; Zhang, Hui

doi:10.1002/prca.201200105

Cited by 14 publications

(14 citation statements)

References 114 publications

(210 reference statements)

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“…NSCLC is, however, a heterogeneous group of neoplasms, with different morphologic subtypes, epigenetic and molecular abnormalities, making targeted therapy and treatment a challenge [ 4 ],[ 6 ],[ 8 ]-[ 10 ]. Therefore, the separation of diverse lung cancer phenotypes and gentotypes, and the identification of novel markers have become critically important for making therapeutic decisions [ 4 ],[ 6 ]-[ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Expression of transcript factors SALL4 and OCT4 in a subset of non-small cell lung carcinomas (NSCLC)

Rodrı́guez

Chen

et al. 2014

Transl Respir Med

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BackgroundSALL4 and OCT4 are transcription factors and play essential roles in stem cell development and oncogenesis. However, the expression of these transcription factors has not been well studied in lung cancers. In this study, we evaluated the expression of SALL4 and OCT4 in non-small cell lung carcinomas (NSCLC) by immunochemistry. NSCLC tissue microarrays (TMAs) were constructed with a total of 77 primary lung adenocarcinomas (ADCs) and 90 primary lung squamous cell carcinomas (SqCCs). A mouse monoclonal anti-human SALL4 (1:400 dilution) and a polyclonal anti-human OCT4 (1:200 dilution) antibodies were used. Nuclear staining of SALL4 and OCT4 was scored semi-quantitatively using a three tiered scale. The expressions of SALL4 and OCT4 were correlated with the tumor differentiation, pathological stage, and patients’ clinical information.ResultsIn primary ADCs, the stronger expression of SALL4 and OCT4 was 7.8% and 9.1%, respectively. The stronger expression of SALL4 was inversely correlated with tumor differentiations. In primary SqCCs, the stronger expressions of SALL4 and OCT4 were 16.7% and 0%, respectively. The expression of SALL4 is correlated with the expression of OCT4, but inversely correlated with the tumor stage in SqCCs.ConclusionsWe found that both SALL4 and OCT4 were differentially expressed in a subset of primary ADC and SqCC. Our finding suggest that different stem cell markers may be expressed and/or play differential role in different subtypes of NSCLC. The potential role of SALL4 and OCT4 needs to be further investigated in NSCLC.

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Section: Introductionmentioning

confidence: 99%

Expression of transcript factors SALL4 and OCT4 in a subset of non-small cell lung carcinomas (NSCLC)

Rodrı́guez

Chen

et al. 2014

Transl Respir Med

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“…That post‐translational protein glycosylation is a quantitatively significant modification is well established as are the roles for these modifications in protein folding, transport of modified proteins to the Golgi, and other intracellular organelles. Glycosylated proteins appear to be excellent targets as biomarkers associated with lung cancer and recent global assessments of the glycoproteome suggest a functional role for these modifications in lung adenocarcinomas . There is emerging evidence that RAGE (receptor for advanced glycation end products), a member of the immunoglobulin superfamily of cell surface receptors in the lung, and its binding ligands (advanced glycation end products) are important in the downstream signaling associated with a number of inflammatory lung diseases including asthma and COPD (for review see ).…”

Section: Resultsmentioning

confidence: 99%

Alterations in the proteome of the respiratory tract in response to single and multiple exposures to naphthalene

Kültz

Sacchi

et al. 2015

Proteomics

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Protein adduction is considered to be critical to the loss of cellular homeostasis associated with environmental chemicals undergoing metabolic activation. Despite considerable effort, our understanding of the key proteins mediating the pathologic consequences from protein modification by electrophiles is incomplete. This work focused on naphthalene-induced acute injury of respiratory epithelial cells and tolerance which arises after multiple toxicant doses to define the initial cellular proteomic response and later protective actions related to tolerance. Airways and nasal olfactory epithelium from mice exposed to 15 ppm NA either for 4 hrs (acute) or for 4 hrs/day × 7 days (tolerant) were used for label free protein quantitation by LC/MS/MS. Cyp2f2 and secretoglobin 1A1 are decreased dramatically in airways of mice exposed for 4 hrs, a finding consistent with the fact that P450's are localized primarily in Clara cells. A number of heat shock proteins and protein disulfide isomerases, which had previously been identified as adduct targets for reactive metabolites from several lung toxicants, were upregulated in airways but not olfactory epithelium of tolerant mice. Protein targets that are upregulated in tolerance may be key players in the pathophysiology associated with reactive metabolite protein adduction.

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“…Quantitative proteomic analysis of BAL fluid has been used to study certain benign lung diseases such as asthma, cystic fibrosis, and interstitial lung disease 18, 19 , but the protein profile in lung cancers has not been well studied 20, 21 . The majority of proteins either secreted from cells or located on extracellular surface of cells are glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

Glycoproteomic Analysis of Bronchoalveolar Lavage (BAL) Fluid Identifies Tumor-Associated Glycoproteins from Lung Adenocarcinoma

Shah

et al. 2013

J. Proteome Res.

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Cytological examination of cells from bronchoalveolar lavage (BAL) is commonly used for the diagnosis of lung cancer. Proteins released from lung cancer cells into BAL may serve as biomarkers for cancer detection. In this study, N-glycoproteins in 8 cases of BAL fluid, as well as 8 lung adenocarcinoma tissues and 8 tumor-matched normal lung tissues, were analyzed using the solid-phase extraction of N-glycoprotein (SPEG), iTRAQ labeling and liquid chromatography tandem mass spectrometry (LC-MS/MS). Of 80 glycoproteins found in BAL specimens, 32 were identified in both cancer BAL and cancer tissues with levels of 25 glycoproteins showing at least a 2-fold difference between cancer and benign BAL. Among them, 8 glycoproteins showed greater than 2-fold elevations in cancer BAL, including Neutrophil elastase (NE), Integrin alpha-M, Cullin-4B, Napsin A, Lysosome-associaed membrane protein 2 (LAMP2), Cathepsin D, BPI fold-containing family B member 2, and Neutrophil gelatinase-associated lipocalin. The levels of Napsin A in cancer BAL were further verified in an independently collected 39 BAL specimens using an ELISA assay. Our study demonstrates that potential protein biomarkers in BAL fluid can be detected and quantified.

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Glycoproteomics using fluid‐based specimens in the discovery of lung cancer protein biomarkers: Promise and challenge

Cited by 14 publications

References 114 publications

Expression of transcript factors SALL4 and OCT4 in a subset of non-small cell lung carcinomas (NSCLC)

Expression of transcript factors SALL4 and OCT4 in a subset of non-small cell lung carcinomas (NSCLC)

Alterations in the proteome of the respiratory tract in response to single and multiple exposures to naphthalene

Glycoproteomic Analysis of Bronchoalveolar Lavage (BAL) Fluid Identifies Tumor-Associated Glycoproteins from Lung Adenocarcinoma

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