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...
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| 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. |
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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.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0122322</identifier><identifier>PMID: 25874882</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Aged ; Biomarkers ; Biomarkers, Tumor - biosynthesis ; Biomarkers, Tumor - genetics ; Calcium ; Calcium-binding protein ; Cancer ; Cell migration ; Cell survival ; Chemotactic Factors - biosynthesis ; Chemotactic Factors - genetics ; Disease ; Drugs ; Female ; Functional analysis ; Gene expression ; Gene Expression Regulation, Neoplastic ; Head & neck cancer ; Hospitals ; Humans ; Immunohistochemistry ; Keratin ; Kinases ; Laryngeal cancer ; Laryngeal Neoplasms - genetics ; Male ; Mass spectrometry ; Mass spectroscopy ; Metastases ; Metastasis ; Middle Aged ; Neck ; Neoplasia ; Neoplasm Metastasis ; Ovarian cancer ; Pharmacy ; Polymerase chain reaction ; Proteins ; Proteomics ; Ribonucleic acid ; RNA ; RNA-mediated interference ; S100 Proteins - biosynthesis ; S100 Proteins - genetics ; Spectroscopy ; Squamous cell carcinoma ; Squamous cells ; Survival ; Tissue Array Analysis ; Tumorigenesis ; Tumors</subject><ispartof>PloS one, 2015-04, Vol.10 (4), p.e0122322-e0122322</ispartof><rights>This is an open access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication: https://creativecommons.org/publicdomain/zero/1.0/ (the “License”) Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-fc8a8cf2f645ad1aa23b926c8a0c69f0709f9a52d599b78a702b7ac28e3f3b173</citedby><cites>FETCH-LOGICAL-c526t-fc8a8cf2f645ad1aa23b926c8a0c69f0709f9a52d599b78a702b7ac28e3f3b173</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4395276/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4395276/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,724,777,781,861,882,2096,2915,23847,27905,27906,53772,53774,79349,79350</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25874882$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Gomes, Cláudio M.</contributor><creatorcontrib>Zha, Cong</creatorcontrib><creatorcontrib>Jiang, Xue Hua</creatorcontrib><creatorcontrib>Peng, Shi Fang</creatorcontrib><title>iTRAQ-based quantitative proteomic analysis on S100 calcium binding protein A2 in metastasis of laryngeal cancer</title><title>PloS one</title><addtitle>PLoS One</addtitle><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.</description><subject>Aged</subject><subject>Biomarkers</subject><subject>Biomarkers, Tumor - biosynthesis</subject><subject>Biomarkers, Tumor - genetics</subject><subject>Calcium</subject><subject>Calcium-binding protein</subject><subject>Cancer</subject><subject>Cell migration</subject><subject>Cell survival</subject><subject>Chemotactic Factors - biosynthesis</subject><subject>Chemotactic Factors - genetics</subject><subject>Disease</subject><subject>Drugs</subject><subject>Female</subject><subject>Functional analysis</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Head & neck cancer</subject><subject>Hospitals</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Keratin</subject><subject>Kinases</subject><subject>Laryngeal cancer</subject><subject>Laryngeal Neoplasms - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zha, Cong</au><au>Jiang, Xue Hua</au><au>Peng, Shi Fang</au><au>Gomes, Cláudio M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>iTRAQ-based quantitative proteomic analysis on S100 calcium binding protein A2 in metastasis of laryngeal cancer</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-04-13</date><risdate>2015</risdate><volume>10</volume><issue>4</issue><spage>e0122322</spage><epage>e0122322</epage><pages>e0122322-e0122322</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25874882</pmid><doi>10.1371/journal.pone.0122322</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Aged Biomarkers Biomarkers, Tumor - biosynthesis Biomarkers, Tumor - genetics Calcium Calcium-binding protein Cancer Cell migration Cell survival Chemotactic Factors - biosynthesis Chemotactic Factors - genetics Disease Drugs Female Functional analysis Gene expression Gene Expression Regulation, Neoplastic Head & neck cancer Hospitals Humans Immunohistochemistry Keratin Kinases Laryngeal cancer Laryngeal Neoplasms - genetics Male Mass spectrometry Mass spectroscopy Metastases Metastasis Middle Aged Neck Neoplasia Neoplasm Metastasis Ovarian cancer Pharmacy Polymerase chain reaction Proteins Proteomics Ribonucleic acid RNA RNA-mediated interference S100 Proteins - biosynthesis S100 Proteins - genetics Spectroscopy Squamous cell carcinoma Squamous cells Survival Tissue Array Analysis Tumorigenesis Tumors |
| title | iTRAQ-based quantitative proteomic analysis on S100 calcium binding protein A2 in metastasis of laryngeal cancer |
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