Quantitative Proteomic Analysis of Differentially Expressed Protein Profiles Involved in Pancreatic Ductal Adenocarcinoma
The aim of this study was to identify differentially expressed proteins among various stages of pancreatic ductal adenocarcinoma (PDAC) by shotgun proteomics using nano-liquid chromatography coupled tandem mass spectrometry and stable isotope dimethyl labeling. Differentially expressed proteins were...
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| Veröffentlicht in: | Pancreas 2016-01, Vol.45 (1), p.71-83 |
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| creator | Kuo, Kung-Kai Kuo, Chao-Jen Chiu, Chiang-Yen Liang, Shih-Shin Huang, Chun-Hao Chi, Shu-Wen Tsai, Kun-Bow Chen, Chiao-Yun Hsi, Edward Cheng, Kuang-Hung Chiou, Shyh-Horng |
| description | The aim of this study was to identify differentially expressed proteins among various stages of pancreatic ductal adenocarcinoma (PDAC) by shotgun proteomics using nano-liquid chromatography coupled tandem mass spectrometry and stable isotope dimethyl labeling.
Differentially expressed proteins were identified and compared based on the mass spectral differences of their isotope-labeled peptide fragments generated from protease digestion.
Our quantitative proteomic analysis of the differentially expressed proteins with stable isotope (deuterium/hydrogen ratio, ≥ 2) identified a total of 353 proteins, with at least 5 protein biomarker proteins that were significantly differentially expressed between cancer and normal mice by at least a 2-fold alteration. These 5 protein biomarker candidates include α-enolase, α-catenin, 14-3-3 β, VDAC1, and calmodulin with high confidence levels. The expression levels were also found to be in agreement with those examined by Western blot and histochemical staining.
The systematic decrease or increase of these identified marker proteins may potentially reflect the morphological aberrations and diseased stages of pancreas carcinoma throughout progressive developments leading to PDAC. The results would form a firm foundation for future work concerning validation and clinical translation of some identified biomarkers into targeted diagnosis and therapy for various stages of PDAC. |
| doi_str_mv | 10.1097/MPA.0000000000000388 |
| format | Article |
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Differentially expressed proteins were identified and compared based on the mass spectral differences of their isotope-labeled peptide fragments generated from protease digestion.
Our quantitative proteomic analysis of the differentially expressed proteins with stable isotope (deuterium/hydrogen ratio, ≥ 2) identified a total of 353 proteins, with at least 5 protein biomarker proteins that were significantly differentially expressed between cancer and normal mice by at least a 2-fold alteration. These 5 protein biomarker candidates include α-enolase, α-catenin, 14-3-3 β, VDAC1, and calmodulin with high confidence levels. The expression levels were also found to be in agreement with those examined by Western blot and histochemical staining.
The systematic decrease or increase of these identified marker proteins may potentially reflect the morphological aberrations and diseased stages of pancreas carcinoma throughout progressive developments leading to PDAC. The results would form a firm foundation for future work concerning validation and clinical translation of some identified biomarkers into targeted diagnosis and therapy for various stages of PDAC.</description><identifier>ISSN: 0885-3177</identifier><identifier>EISSN: 1536-4828</identifier><identifier>DOI: 10.1097/MPA.0000000000000388</identifier><identifier>PMID: 26262590</identifier><language>eng</language><publisher>United States: Lippincott Williams & Wilkins</publisher><subject>Animals ; Biomarkers, Tumor - genetics ; Biomarkers, Tumor - metabolism ; Carcinoma, Pancreatic Ductal - genetics ; Carcinoma, Pancreatic Ductal - metabolism ; Carcinoma, Pancreatic Ductal - pathology ; Chromatography, Liquid ; Computational Biology ; Databases, Protein ; Disease Models, Animal ; Genetic Predisposition to Disease ; Isotope Labeling ; Mice ; Mice, Transgenic ; Nanotechnology ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Neoplasm Staging ; Original ; Pancreatic Neoplasms - genetics ; Pancreatic Neoplasms - metabolism ; Pancreatic Neoplasms - pathology ; Peptide Mapping ; Phenotype ; Protein Interaction Maps ; Proteomics - methods ; Tandem Mass Spectrometry ; Time Factors</subject><ispartof>Pancreas, 2016-01, Vol.45 (1), p.71-83</ispartof><rights>Copyright © 2015 Wolters Kluwer Health, Inc. All rights reserved. 2015 Wolters Kluwer Health, Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c408t-42072d903219884045deb3673894398c7aa493f216a77947def0d0a1cc0148b13</citedby><cites>FETCH-LOGICAL-c408t-42072d903219884045deb3673894398c7aa493f216a77947def0d0a1cc0148b13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26262590$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kuo, Kung-Kai</creatorcontrib><creatorcontrib>Kuo, Chao-Jen</creatorcontrib><creatorcontrib>Chiu, Chiang-Yen</creatorcontrib><creatorcontrib>Liang, Shih-Shin</creatorcontrib><creatorcontrib>Huang, Chun-Hao</creatorcontrib><creatorcontrib>Chi, Shu-Wen</creatorcontrib><creatorcontrib>Tsai, Kun-Bow</creatorcontrib><creatorcontrib>Chen, Chiao-Yun</creatorcontrib><creatorcontrib>Hsi, Edward</creatorcontrib><creatorcontrib>Cheng, Kuang-Hung</creatorcontrib><creatorcontrib>Chiou, Shyh-Horng</creatorcontrib><title>Quantitative Proteomic Analysis of Differentially Expressed Protein Profiles Involved in Pancreatic Ductal Adenocarcinoma</title><title>Pancreas</title><addtitle>Pancreas</addtitle><description>The aim of this study was to identify differentially expressed proteins among various stages of pancreatic ductal adenocarcinoma (PDAC) by shotgun proteomics using nano-liquid chromatography coupled tandem mass spectrometry and stable isotope dimethyl labeling.
Differentially expressed proteins were identified and compared based on the mass spectral differences of their isotope-labeled peptide fragments generated from protease digestion.
Our quantitative proteomic analysis of the differentially expressed proteins with stable isotope (deuterium/hydrogen ratio, ≥ 2) identified a total of 353 proteins, with at least 5 protein biomarker proteins that were significantly differentially expressed between cancer and normal mice by at least a 2-fold alteration. These 5 protein biomarker candidates include α-enolase, α-catenin, 14-3-3 β, VDAC1, and calmodulin with high confidence levels. The expression levels were also found to be in agreement with those examined by Western blot and histochemical staining.
The systematic decrease or increase of these identified marker proteins may potentially reflect the morphological aberrations and diseased stages of pancreas carcinoma throughout progressive developments leading to PDAC. The results would form a firm foundation for future work concerning validation and clinical translation of some identified biomarkers into targeted diagnosis and therapy for various stages of PDAC.</description><subject>Animals</subject><subject>Biomarkers, Tumor - genetics</subject><subject>Biomarkers, Tumor - metabolism</subject><subject>Carcinoma, Pancreatic Ductal - genetics</subject><subject>Carcinoma, Pancreatic Ductal - metabolism</subject><subject>Carcinoma, Pancreatic Ductal - pathology</subject><subject>Chromatography, Liquid</subject><subject>Computational Biology</subject><subject>Databases, Protein</subject><subject>Disease Models, Animal</subject><subject>Genetic Predisposition to Disease</subject><subject>Isotope Labeling</subject><subject>Mice</subject><subject>Mice, Transgenic</subject><subject>Nanotechnology</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Neoplasm Staging</subject><subject>Original</subject><subject>Pancreatic Neoplasms - genetics</subject><subject>Pancreatic Neoplasms - metabolism</subject><subject>Pancreatic Neoplasms - pathology</subject><subject>Peptide Mapping</subject><subject>Phenotype</subject><subject>Protein Interaction Maps</subject><subject>Proteomics - methods</subject><subject>Tandem Mass Spectrometry</subject><subject>Time Factors</subject><issn>0885-3177</issn><issn>1536-4828</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdUU1vFDEMjRCILoV_gNAcuUybr5kkF6RVW6BSEUWCc-TNeCAokyzJzKr778lq26pgHyz5PT_beoS8ZfSMUaPOv9yuz-jTEFo_IyvWib6VmuvnZEW17lrBlDohr0r5TSlTojMvyQnva3aGrsj-2wJx9jPMfofNbU4zpsm7Zh0h7IsvTRqbSz-OmLHSIIR9c3W3zVgKDke6j4c6-oCluY67FHYVOTQhuoxV1zWXi5shNOsBY3KQnY9pgtfkxQih4Jv7ekp-fLz6fvG5vfn66fpifdM6SfXcSk4VHwwVnBmtJZXdgBvRK6GNFEY7BSCNGDnrQSkj1YAjHSgw5yiTesPEKflw1N0umwkHV__IEOw2-wny3ibw9l8k-l_2Z9pZ2SvVGVMF3t8L5PRnwTLbyReHIUDEtBTLlDQ955LLSpVHqsuplIzj4xpG7cE1W12z_7tWx949PfFx6MEm8RfQMJUk</recordid><startdate>20160101</startdate><enddate>20160101</enddate><creator>Kuo, Kung-Kai</creator><creator>Kuo, Chao-Jen</creator><creator>Chiu, Chiang-Yen</creator><creator>Liang, Shih-Shin</creator><creator>Huang, Chun-Hao</creator><creator>Chi, Shu-Wen</creator><creator>Tsai, Kun-Bow</creator><creator>Chen, Chiao-Yun</creator><creator>Hsi, Edward</creator><creator>Cheng, Kuang-Hung</creator><creator>Chiou, Shyh-Horng</creator><general>Lippincott Williams & Wilkins</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20160101</creationdate><title>Quantitative Proteomic Analysis of Differentially Expressed Protein Profiles Involved in Pancreatic Ductal Adenocarcinoma</title><author>Kuo, Kung-Kai ; Kuo, Chao-Jen ; Chiu, Chiang-Yen ; Liang, Shih-Shin ; Huang, Chun-Hao ; Chi, Shu-Wen ; Tsai, Kun-Bow ; Chen, Chiao-Yun ; Hsi, Edward ; Cheng, Kuang-Hung ; Chiou, Shyh-Horng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c408t-42072d903219884045deb3673894398c7aa493f216a77947def0d0a1cc0148b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Biomarkers, Tumor - genetics</topic><topic>Biomarkers, Tumor - metabolism</topic><topic>Carcinoma, Pancreatic Ductal - genetics</topic><topic>Carcinoma, Pancreatic Ductal - metabolism</topic><topic>Carcinoma, Pancreatic Ductal - pathology</topic><topic>Chromatography, Liquid</topic><topic>Computational Biology</topic><topic>Databases, Protein</topic><topic>Disease Models, Animal</topic><topic>Genetic Predisposition to Disease</topic><topic>Isotope Labeling</topic><topic>Mice</topic><topic>Mice, Transgenic</topic><topic>Nanotechnology</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Neoplasm Staging</topic><topic>Original</topic><topic>Pancreatic Neoplasms - genetics</topic><topic>Pancreatic Neoplasms - metabolism</topic><topic>Pancreatic Neoplasms - pathology</topic><topic>Peptide Mapping</topic><topic>Phenotype</topic><topic>Protein Interaction Maps</topic><topic>Proteomics - methods</topic><topic>Tandem Mass Spectrometry</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kuo, Kung-Kai</creatorcontrib><creatorcontrib>Kuo, Chao-Jen</creatorcontrib><creatorcontrib>Chiu, Chiang-Yen</creatorcontrib><creatorcontrib>Liang, Shih-Shin</creatorcontrib><creatorcontrib>Huang, Chun-Hao</creatorcontrib><creatorcontrib>Chi, Shu-Wen</creatorcontrib><creatorcontrib>Tsai, Kun-Bow</creatorcontrib><creatorcontrib>Chen, Chiao-Yun</creatorcontrib><creatorcontrib>Hsi, Edward</creatorcontrib><creatorcontrib>Cheng, Kuang-Hung</creatorcontrib><creatorcontrib>Chiou, Shyh-Horng</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Pancreas</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kuo, Kung-Kai</au><au>Kuo, Chao-Jen</au><au>Chiu, Chiang-Yen</au><au>Liang, Shih-Shin</au><au>Huang, Chun-Hao</au><au>Chi, Shu-Wen</au><au>Tsai, Kun-Bow</au><au>Chen, Chiao-Yun</au><au>Hsi, Edward</au><au>Cheng, Kuang-Hung</au><au>Chiou, Shyh-Horng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative Proteomic Analysis of Differentially Expressed Protein Profiles Involved in Pancreatic Ductal Adenocarcinoma</atitle><jtitle>Pancreas</jtitle><addtitle>Pancreas</addtitle><date>2016-01-01</date><risdate>2016</risdate><volume>45</volume><issue>1</issue><spage>71</spage><epage>83</epage><pages>71-83</pages><issn>0885-3177</issn><eissn>1536-4828</eissn><abstract>The aim of this study was to identify differentially expressed proteins among various stages of pancreatic ductal adenocarcinoma (PDAC) by shotgun proteomics using nano-liquid chromatography coupled tandem mass spectrometry and stable isotope dimethyl labeling.
Differentially expressed proteins were identified and compared based on the mass spectral differences of their isotope-labeled peptide fragments generated from protease digestion.
Our quantitative proteomic analysis of the differentially expressed proteins with stable isotope (deuterium/hydrogen ratio, ≥ 2) identified a total of 353 proteins, with at least 5 protein biomarker proteins that were significantly differentially expressed between cancer and normal mice by at least a 2-fold alteration. These 5 protein biomarker candidates include α-enolase, α-catenin, 14-3-3 β, VDAC1, and calmodulin with high confidence levels. The expression levels were also found to be in agreement with those examined by Western blot and histochemical staining.
The systematic decrease or increase of these identified marker proteins may potentially reflect the morphological aberrations and diseased stages of pancreas carcinoma throughout progressive developments leading to PDAC. The results would form a firm foundation for future work concerning validation and clinical translation of some identified biomarkers into targeted diagnosis and therapy for various stages of PDAC.</abstract><cop>United States</cop><pub>Lippincott Williams & Wilkins</pub><pmid>26262590</pmid><doi>10.1097/MPA.0000000000000388</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Pancreas, 2016-01, Vol.45 (1), p.71-83 |
| issn | 0885-3177 1536-4828 |
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| subjects | Animals Biomarkers, Tumor - genetics Biomarkers, Tumor - metabolism Carcinoma, Pancreatic Ductal - genetics Carcinoma, Pancreatic Ductal - metabolism Carcinoma, Pancreatic Ductal - pathology Chromatography, Liquid Computational Biology Databases, Protein Disease Models, Animal Genetic Predisposition to Disease Isotope Labeling Mice Mice, Transgenic Nanotechnology Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Neoplasm Staging Original Pancreatic Neoplasms - genetics Pancreatic Neoplasms - metabolism Pancreatic Neoplasms - pathology Peptide Mapping Phenotype Protein Interaction Maps Proteomics - methods Tandem Mass Spectrometry Time Factors |
| title | Quantitative Proteomic Analysis of Differentially Expressed Protein Profiles Involved in Pancreatic Ductal Adenocarcinoma |
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