ArticleTumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine2016
iTRAQ-based quantitative proteomic analysis of esophageal squamous cell carcinoma.
Article in Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- The role of Prolyl 3-Hydroxylase 1 (P3H1) in tumor development and prognosis: a pan-cancer analysis with validation in colonic adenocarcinoma.American journal of translational research · 2025Article
- Deciphering Cancer Complexity: Integrative Proteogenomics and Proteomics Approaches for Biomarker Discovery.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Molecular Characterization of Esophageal Squamous Cell Carcinoma Using Quantitative Proteomics.Cancers · 2023Article
- A metabolomic and proteomic study to elucidate the molecular mechanisms of immunotherapy resistance in patients with oesophageal squamous cell carcinoma.Biomedical reports · 2023Article
- Prognostic Value of GPNMB, EGFR, p-PI3K, and Ki-67 in Patients with Esophageal Squamous Cell Carcinoma.Analytical cellular pathology (Amsterdam) · 2022Article
- Target identification of natural medicine with chemical proteomics approach: probe synthesis, target fishing and protein identification.Signal transduction and targeted therapy · 2020Review
- Expression, regulation and targeting of receptor tyrosine kinases in esophageal squamous cell carcinoma.Molecular cancer · 2018Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Esophageal squamous cell carcinoma (ESCC) is one of the most common cancers. In this study, our objective was to identify differentially regulated proteins in ESCC using isobaric tag for relative and absolute quantification (iTRAQ) technique and liquid chromatography-tandem mass spectrometry (LC-MS/MS). We compared the protein expression profiles of ESCC tumor tissues with the corresponding adjacent normal tissue from three patients. It was determined that 72 and 57 unique proteins were significantly up-regulated and down-regulated in all three samples. In addition, there were 431 significantly differentially regulated proteins having at least two biological samples. This subject found some of the differential proteins, such as prolyl 4-hydroxylase subunit alpha-1, prolyl 4-hydroxylase subunit alpha-2, and calponin-2, immunoglobulin superfamily containing leucine-rich repeat protein, and prolyl 3-hydroxylase1, which were few studies about them in ESCC. In order to determine the results, we performed another independent experiment. Our results indicated quantitative proteomics, as a robust discovery tool for the identification, differentially regulated proteins in cancers.
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Registered trials
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