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iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer
Laryngeal cancer is the most frequent neoplasm in the head and neck region, with the vast majority of tumors originating from squamous cells. The survival rate of patients with laryngeal cancer has not improved substantially over the past 25 years. To acquire further knowledge regarding the molecule...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4395276/ https://www.ncbi.nlm.nih.gov/pubmed/25874882 http://dx.doi.org/10.1371/journal.pone.0122322 |
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author | Zha, Cong Jiang, Xue Hua Peng, Shi Fang |
author_facet | Zha, Cong Jiang, Xue Hua Peng, Shi Fang |
author_sort | Zha, Cong |
collection | PubMed |
description | Laryngeal cancer is the most frequent neoplasm in the head and neck region, with the vast majority of tumors originating from squamous cells. The survival rate of patients with laryngeal cancer has not improved substantially over the past 25 years. To acquire further knowledge regarding the molecules responsible for laryngeal cancer oncogenesis and, in turn, to improve target therapy,iTRAQ and mass spectrometry analysis were utilized to detect differences in protein expression from 15 paired laryngeal cancer and adjacent non-cancerous tissue samples. Using mass spectrometry analysis, the expression levels of 100 proteins in laryngeal cancer samples were distinct from the non-tumor, non-cancerous samples. Further validation of the differentially expressed proteins S100A2, KRT16, FGB and HSPB1 were carried out using quantitative real-time RT-PCR, immunoblot and immunohistochemistry. Functional analysis of one of the highly expressed proteins, S100 calcium binding protein A2 (S100A2), was performed using RNA interference. As a consequence, attenuated S100A2 expression enhanced the ability of HEp-2 cell lines to migrate and invade in vitro. Our investigation complements the current understanding of laryngeal cancer progression. Furthermore, this study supports the concept that enhanced expression of S100A2 may be a promising strategy in developing novel cancer therapeutic drugs. |
format | Online Article Text |
id | pubmed-4395276 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-43952762015-04-21 iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer Zha, Cong Jiang, Xue Hua Peng, Shi Fang PLoS One Research Article Laryngeal cancer is the most frequent neoplasm in the head and neck region, with the vast majority of tumors originating from squamous cells. The survival rate of patients with laryngeal cancer has not improved substantially over the past 25 years. To acquire further knowledge regarding the molecules responsible for laryngeal cancer oncogenesis and, in turn, to improve target therapy,iTRAQ and mass spectrometry analysis were utilized to detect differences in protein expression from 15 paired laryngeal cancer and adjacent non-cancerous tissue samples. Using mass spectrometry analysis, the expression levels of 100 proteins in laryngeal cancer samples were distinct from the non-tumor, non-cancerous samples. Further validation of the differentially expressed proteins S100A2, KRT16, FGB and HSPB1 were carried out using quantitative real-time RT-PCR, immunoblot and immunohistochemistry. Functional analysis of one of the highly expressed proteins, S100 calcium binding protein A2 (S100A2), was performed using RNA interference. As a consequence, attenuated S100A2 expression enhanced the ability of HEp-2 cell lines to migrate and invade in vitro. Our investigation complements the current understanding of laryngeal cancer progression. Furthermore, this study supports the concept that enhanced expression of S100A2 may be a promising strategy in developing novel cancer therapeutic drugs. Public Library of Science 2015-04-13 /pmc/articles/PMC4395276/ /pubmed/25874882 http://dx.doi.org/10.1371/journal.pone.0122322 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. |
spellingShingle | Research Article Zha, Cong Jiang, Xue Hua Peng, Shi Fang iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer |
title | iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer |
title_full | iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer |
title_fullStr | iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer |
title_full_unstemmed | iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer |
title_short | iTRAQ-Based Quantitative Proteomic Analysis on S100 Calcium Binding Protein A2 in Metastasis of Laryngeal Cancer |
title_sort | itraq-based quantitative proteomic analysis on s100 calcium binding protein a2 in metastasis of laryngeal cancer |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4395276/ https://www.ncbi.nlm.nih.gov/pubmed/25874882 http://dx.doi.org/10.1371/journal.pone.0122322 |
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