Comparative Profiling of Triple-Negative Breast Carcinomas Tissue Glycoproteome by Sequential Purification of Glycoproteins and Stable Isotope Labeling
Background: Women with triple negative breast cancers (TNBCs) have a poor prognosis due to lack of suitable targeted therapies. Changes in the protein glycosylation are increasingly being recognized as an important modification associated with cancer etiology. Methods: In an attempt to identify TNBC...
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| Veröffentlicht in: | Cellular Physiology and Biochemistry 2016-01, Vol.38 (1), p.110-121 |
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| container_title | Cellular Physiology and Biochemistry |
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| creator | Chen, Xiang Wu, Jindao Huang, Huaxing Ding, Qiang Liu, Xiaoan Chen, Lin Zha, Xiaoming Liang, Mengdi He, Jing Zhu, Qiannan Wang, Shui Xia, Tiansong |
| description | Background: Women with triple negative breast cancers (TNBCs) have a poor prognosis due to lack of suitable targeted therapies. Changes in the protein glycosylation are increasingly being recognized as an important modification associated with cancer etiology. Methods: In an attempt to identify TNBC biomarkers with greater diagnostic and prognostic capabilities, hydrazide- based chemistry method combined with LC-MS/MS were used to purify and identify N-linked glycopeptides or glycoproteins of tissues from TNBC patients. Results: A total of 550 unique N-linked glycoproteins were identified, among these proteins, 72 unique N-linked glycoproteins were significantly regulated in tumor tissues, of which 56 proteins were upregulated and 16 proteins were downregulated. To assess the validity of the results, three selected proteins including Vascular endothelial growth factor receptor 1, Insulin receptor, Tissue factor pathway inhibitor were selected for western blot analysis, and these proteins were found as potential biomarkers of TNBC. The top three pathways of differentially expressed glycoproteins participated in were caveolar-mediated endocytosis signaling, agrin interactions at neuromuscular junction and LXR/RXR activation. Conclusion: This work provides potential glycoprotein markers to function as a novel tissue-based biomarker for TNBC. |
| doi_str_mv | 10.1159/000438613 |
| format | Article |
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Changes in the protein glycosylation are increasingly being recognized as an important modification associated with cancer etiology. Methods: In an attempt to identify TNBC biomarkers with greater diagnostic and prognostic capabilities, hydrazide- based chemistry method combined with LC-MS/MS were used to purify and identify N-linked glycopeptides or glycoproteins of tissues from TNBC patients. Results: A total of 550 unique N-linked glycoproteins were identified, among these proteins, 72 unique N-linked glycoproteins were significantly regulated in tumor tissues, of which 56 proteins were upregulated and 16 proteins were downregulated. To assess the validity of the results, three selected proteins including Vascular endothelial growth factor receptor 1, Insulin receptor, Tissue factor pathway inhibitor were selected for western blot analysis, and these proteins were found as potential biomarkers of TNBC. The top three pathways of differentially expressed glycoproteins participated in were caveolar-mediated endocytosis signaling, agrin interactions at neuromuscular junction and LXR/RXR activation. Conclusion: This work provides potential glycoprotein markers to function as a novel tissue-based biomarker for TNBC.</description><identifier>ISSN: 1015-8987</identifier><identifier>EISSN: 1421-9778</identifier><identifier>DOI: 10.1159/000438613</identifier><identifier>PMID: 26742121</identifier><language>eng</language><publisher>Basel, Switzerland: S. Karger AG</publisher><subject>Adult ; Aged ; Aged, 80 and over ; Biomarkers, Tumor - metabolism ; Breast cancer ; Chromatography, High Pressure Liquid ; Comparative analysis ; Diagnosis ; Dimethyl Labelling ; Female ; Glycopeptides - analysis ; Glycoproteins ; Glycoproteins - metabolism ; Glycoproteome ; Health aspects ; Humans ; Isotope Labeling ; Lipoproteins - metabolism ; Metabolic Networks and Pathways ; Middle Aged ; Original Paper ; Prognosis ; Proteomics ; Receptor, Insulin - metabolism ; Risk factors ; Tandem Mass Spectrometry ; Triple Negative Breast Neoplasms - metabolism ; Triple Negative Breast Neoplasms - pathology ; Triple-negative Breast Carcinomas ; Vascular Endothelial Growth Factor Receptor-1 - metabolism</subject><ispartof>Cellular Physiology and Biochemistry, 2016-01, Vol.38 (1), p.110-121</ispartof><rights>2016 The Author(s) Published by S. Karger AG, Basel</rights><rights>2016 The Author(s) Published by S. Karger AG, Basel.</rights><rights>COPYRIGHT 2016 S. Karger AG</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c502t-17a52c29bdce000666ea897098500c3e258da593739faf3d40670582dc63694d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,860,2095,27614,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26742121$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Xiang</creatorcontrib><creatorcontrib>Wu, Jindao</creatorcontrib><creatorcontrib>Huang, Huaxing</creatorcontrib><creatorcontrib>Ding, Qiang</creatorcontrib><creatorcontrib>Liu, Xiaoan</creatorcontrib><creatorcontrib>Chen, Lin</creatorcontrib><creatorcontrib>Zha, Xiaoming</creatorcontrib><creatorcontrib>Liang, Mengdi</creatorcontrib><creatorcontrib>He, Jing</creatorcontrib><creatorcontrib>Zhu, Qiannan</creatorcontrib><creatorcontrib>Wang, Shui</creatorcontrib><creatorcontrib>Xia, Tiansong</creatorcontrib><title>Comparative Profiling of Triple-Negative Breast Carcinomas Tissue Glycoproteome by Sequential Purification of Glycoproteins and Stable Isotope Labeling</title><title>Cellular Physiology and Biochemistry</title><addtitle>Cell Physiol Biochem</addtitle><description>Background: Women with triple negative breast cancers (TNBCs) have a poor prognosis due to lack of suitable targeted therapies. Changes in the protein glycosylation are increasingly being recognized as an important modification associated with cancer etiology. Methods: In an attempt to identify TNBC biomarkers with greater diagnostic and prognostic capabilities, hydrazide- based chemistry method combined with LC-MS/MS were used to purify and identify N-linked glycopeptides or glycoproteins of tissues from TNBC patients. Results: A total of 550 unique N-linked glycoproteins were identified, among these proteins, 72 unique N-linked glycoproteins were significantly regulated in tumor tissues, of which 56 proteins were upregulated and 16 proteins were downregulated. To assess the validity of the results, three selected proteins including Vascular endothelial growth factor receptor 1, Insulin receptor, Tissue factor pathway inhibitor were selected for western blot analysis, and these proteins were found as potential biomarkers of TNBC. The top three pathways of differentially expressed glycoproteins participated in were caveolar-mediated endocytosis signaling, agrin interactions at neuromuscular junction and LXR/RXR activation. Conclusion: This work provides potential glycoprotein markers to function as a novel tissue-based biomarker for TNBC.</description><subject>Adult</subject><subject>Aged</subject><subject>Aged, 80 and over</subject><subject>Biomarkers, Tumor - metabolism</subject><subject>Breast cancer</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Comparative analysis</subject><subject>Diagnosis</subject><subject>Dimethyl Labelling</subject><subject>Female</subject><subject>Glycopeptides - analysis</subject><subject>Glycoproteins</subject><subject>Glycoproteins - metabolism</subject><subject>Glycoproteome</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Isotope Labeling</subject><subject>Lipoproteins - metabolism</subject><subject>Metabolic Networks and Pathways</subject><subject>Middle Aged</subject><subject>Original Paper</subject><subject>Prognosis</subject><subject>Proteomics</subject><subject>Receptor, Insulin - metabolism</subject><subject>Risk factors</subject><subject>Tandem Mass Spectrometry</subject><subject>Triple Negative Breast Neoplasms - metabolism</subject><subject>Triple Negative Breast Neoplasms - pathology</subject><subject>Triple-negative Breast Carcinomas</subject><subject>Vascular Endothelial Growth Factor Receptor-1 - metabolism</subject><issn>1015-8987</issn><issn>1421-9778</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>M--</sourceid><sourceid>EIF</sourceid><sourceid>DOA</sourceid><recordid>eNptkk1v1DAQhiMEoqVw4I6QpV7gkOLYsZ0c2xWUlSpYqcvZmtjjlUsSBzuLtL-Ev4uXlOWCfPDHPPPOeGaK4nVFr6pKtB8opTVvZMWfFOdVzaqyVap5ms-0EmXTNuqseJHSA81X1bLnxRmTKmOsOi9-rcIwQYTZ_0SyicH53o87EhzZRj_1WH7B3WK8iQhpJiuIxo9hgES2PqU9ktv-YMIUw4xhQNIdyD3-2OM4e-jJZh-98yYrhPEo-o_1YyIwWnI_Q9cjWacwhwnJHXR4zOBl8cxBn_DV435RfPv0cbv6XN59vV2vru9KIyiby0qBYIa1nTWYqyClRGhaRdtGUGo4MtFYEC1XvHXguK2pVFQ0zBrJZVtbflGsF10b4EFP0Q8QDzqA138eQtxpiLM3PeqOInfQMpnV6hyzAcY6J8DU1FIuRdZ6t2jlD-YKpFkPPhnsexgx7JOulGSUCVk3Gb1a0B1kZT-6MEcweVkcvAkj5j6gvs6hBOW1Omq_XxxMDClFdKdcK6qPQ6BPQ5DZt4957LsB7Yn82_UMvFmA7xB3GE_Ayf_yv-bV5mYh9GQd_w0TgcHJ</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Chen, Xiang</creator><creator>Wu, Jindao</creator><creator>Huang, Huaxing</creator><creator>Ding, Qiang</creator><creator>Liu, Xiaoan</creator><creator>Chen, Lin</creator><creator>Zha, Xiaoming</creator><creator>Liang, Mengdi</creator><creator>He, Jing</creator><creator>Zhu, Qiannan</creator><creator>Wang, Shui</creator><creator>Xia, Tiansong</creator><general>S. Karger AG</general><general>Cell Physiol Biochem Press GmbH & Co KG</general><scope>M--</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IAO</scope><scope>7X8</scope><scope>DOA</scope></search><sort><creationdate>20160101</creationdate><title>Comparative Profiling of Triple-Negative Breast Carcinomas Tissue Glycoproteome by Sequential Purification of Glycoproteins and Stable Isotope Labeling</title><author>Chen, Xiang ; Wu, Jindao ; Huang, Huaxing ; Ding, Qiang ; Liu, Xiaoan ; Chen, Lin ; Zha, Xiaoming ; Liang, Mengdi ; He, Jing ; Zhu, Qiannan ; Wang, Shui ; Xia, Tiansong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c502t-17a52c29bdce000666ea897098500c3e258da593739faf3d40670582dc63694d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Adult</topic><topic>Aged</topic><topic>Aged, 80 and over</topic><topic>Biomarkers, Tumor - metabolism</topic><topic>Breast cancer</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Comparative analysis</topic><topic>Diagnosis</topic><topic>Dimethyl Labelling</topic><topic>Female</topic><topic>Glycopeptides - analysis</topic><topic>Glycoproteins</topic><topic>Glycoproteins - metabolism</topic><topic>Glycoproteome</topic><topic>Health aspects</topic><topic>Humans</topic><topic>Isotope Labeling</topic><topic>Lipoproteins - metabolism</topic><topic>Metabolic Networks and Pathways</topic><topic>Middle Aged</topic><topic>Original Paper</topic><topic>Prognosis</topic><topic>Proteomics</topic><topic>Receptor, Insulin - metabolism</topic><topic>Risk factors</topic><topic>Tandem Mass Spectrometry</topic><topic>Triple Negative Breast Neoplasms - metabolism</topic><topic>Triple Negative Breast Neoplasms - pathology</topic><topic>Triple-negative Breast Carcinomas</topic><topic>Vascular Endothelial Growth Factor Receptor-1 - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Xiang</creatorcontrib><creatorcontrib>Wu, Jindao</creatorcontrib><creatorcontrib>Huang, Huaxing</creatorcontrib><creatorcontrib>Ding, Qiang</creatorcontrib><creatorcontrib>Liu, Xiaoan</creatorcontrib><creatorcontrib>Chen, Lin</creatorcontrib><creatorcontrib>Zha, Xiaoming</creatorcontrib><creatorcontrib>Liang, Mengdi</creatorcontrib><creatorcontrib>He, Jing</creatorcontrib><creatorcontrib>Zhu, Qiannan</creatorcontrib><creatorcontrib>Wang, Shui</creatorcontrib><creatorcontrib>Xia, Tiansong</creatorcontrib><collection>Karger Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale Academic OneFile</collection><collection>MEDLINE - Academic</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Cellular Physiology and Biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Xiang</au><au>Wu, Jindao</au><au>Huang, Huaxing</au><au>Ding, Qiang</au><au>Liu, Xiaoan</au><au>Chen, Lin</au><au>Zha, Xiaoming</au><au>Liang, Mengdi</au><au>He, Jing</au><au>Zhu, Qiannan</au><au>Wang, Shui</au><au>Xia, Tiansong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative Profiling of Triple-Negative Breast Carcinomas Tissue Glycoproteome by Sequential Purification of Glycoproteins and Stable Isotope Labeling</atitle><jtitle>Cellular Physiology and Biochemistry</jtitle><addtitle>Cell Physiol Biochem</addtitle><date>2016-01-01</date><risdate>2016</risdate><volume>38</volume><issue>1</issue><spage>110</spage><epage>121</epage><pages>110-121</pages><issn>1015-8987</issn><eissn>1421-9778</eissn><abstract>Background: Women with triple negative breast cancers (TNBCs) have a poor prognosis due to lack of suitable targeted therapies. Changes in the protein glycosylation are increasingly being recognized as an important modification associated with cancer etiology. Methods: In an attempt to identify TNBC biomarkers with greater diagnostic and prognostic capabilities, hydrazide- based chemistry method combined with LC-MS/MS were used to purify and identify N-linked glycopeptides or glycoproteins of tissues from TNBC patients. Results: A total of 550 unique N-linked glycoproteins were identified, among these proteins, 72 unique N-linked glycoproteins were significantly regulated in tumor tissues, of which 56 proteins were upregulated and 16 proteins were downregulated. To assess the validity of the results, three selected proteins including Vascular endothelial growth factor receptor 1, Insulin receptor, Tissue factor pathway inhibitor were selected for western blot analysis, and these proteins were found as potential biomarkers of TNBC. The top three pathways of differentially expressed glycoproteins participated in were caveolar-mediated endocytosis signaling, agrin interactions at neuromuscular junction and LXR/RXR activation. Conclusion: This work provides potential glycoprotein markers to function as a novel tissue-based biomarker for TNBC.</abstract><cop>Basel, Switzerland</cop><pub>S. Karger AG</pub><pmid>26742121</pmid><doi>10.1159/000438613</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adult Aged Aged, 80 and over Biomarkers, Tumor - metabolism Breast cancer Chromatography, High Pressure Liquid Comparative analysis Diagnosis Dimethyl Labelling Female Glycopeptides - analysis Glycoproteins Glycoproteins - metabolism Glycoproteome Health aspects Humans Isotope Labeling Lipoproteins - metabolism Metabolic Networks and Pathways Middle Aged Original Paper Prognosis Proteomics Receptor, Insulin - metabolism Risk factors Tandem Mass Spectrometry Triple Negative Breast Neoplasms - metabolism Triple Negative Breast Neoplasms - pathology Triple-negative Breast Carcinomas Vascular Endothelial Growth Factor Receptor-1 - metabolism |
| title | Comparative Profiling of Triple-Negative Breast Carcinomas Tissue Glycoproteome by Sequential Purification of Glycoproteins and Stable Isotope Labeling |
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