Proteomic analysis of lymph
Identifieur interne : 004036 ( Istex/Corpus ); précédent : 004035; suivant : 004037Proteomic analysis of lymph
Auteurs : Lee V. Leak ; Lance A. Liotta ; Henry Krutzsch ; Michael Jones ; Vincent A. Fusaroa ; Sally J. Ross ; Yingming Zhao ; Emanuel F. Petricoin IiiSource :
- PROTEOMICS [ 1615-9853 ] ; 2004-03.
Abstract
This report provides the first proteomic analysis of normal ovine lymph. By establishing the fact that lymph is more than an ultrafiltrate of blood plasma, it documents that the lymph proteome contains an array of proteins that differentiates it from plasma. The protein chip technology, surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry (SELDI‐TOF‐MS), two‐dimensional gel electrophoresis (2‐D PAGE) and MS, were employed to examine the protein expression profiles of ovine lymph. Using a weak cation exchange chip surface to assay lymph and plasma samples by SELDI‐TOF‐MS showed that the analysis of peak maps from lymph contained three protein peaks that were found only in lymph, while analysis of peak maps from plasma samples showed that five protein peaks were found only in plasma. Lymph and plasma samples showed eight peaks that were common to both. There were also more ions present in plasma than in lymph, which is consistent with the 2‐D PAGE analysis. MS analysis of a large number of protein spots from 2‐D PAGE gels of lymph produced MS/MS sequences for 18 proteins that were identified by searching against a comprehensive protein sequence database. As in plasma, large protein spots of albumin dominated the protein pattern in lymph. Other major proteins identified in 2‐D PAGE gels of lymph included, fibrinogen α‐ and β‐chains, immunoglobulin G (IgG) heavy chain, serotransferrin precursor, lactoferrin, and apolipoprotein A‐1. Two proteins that were identified and were differentially expressed in lymph were glial fibrillary astrocyte acidic protein and neutrophil cytosol factor‐1. By bringing the technologies of proteomics to bear on the analysis of lymph, it is possible to detect proteins in lymph that are quantitatively and qualitatively differentially expressed from those of plasma.
Url:
DOI: 10.1002/pmic.200300573
Links to Exploration step
ISTEX:88529F567434F379288B348301A6C18FDDD060E0Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Proteomic analysis of lymph</title><author><name sortKey="Leak, Lee V" sort="Leak, Lee V" uniqKey="Leak L" first="Lee V." last="Leak">Lee V. Leak</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Ernest E. Just Laboratory of Cellular Biology, College of Medicine, Howard University, Washington, DC, USA</mods:affiliation></affiliation></author><author><name sortKey="Liotta, Lance A" sort="Liotta, Lance A" uniqKey="Liotta L" first="Lance A." last="Liotta">Lance A. Liotta</name><affiliation><mods:affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Krutzsch, Henry" sort="Krutzsch, Henry" uniqKey="Krutzsch H" first="Henry" last="Krutzsch">Henry Krutzsch</name><affiliation><mods:affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Jones, Michael" sort="Jones, Michael" uniqKey="Jones M" first="Michael" last="Jones">Michael Jones</name><affiliation><mods:affiliation>Laboratory of Animal Surgery, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Fusaroa, Vincent A" sort="Fusaroa, Vincent A" uniqKey="Fusaroa V" first="Vincent A." last="Fusaroa">Vincent A. Fusaroa</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Ross, Sally J" sort="Ross, Sally J" uniqKey="Ross S" first="Sally J." last="Ross">Sally J. Ross</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Zhao, Yingming" sort="Zhao, Yingming" uniqKey="Zhao Y" first="Yingming" last="Zhao">Yingming Zhao</name><affiliation><mods:affiliation>Department of Biochemistry, U. T. Southwestern Medical Center, Dallas, TX, USA</mods:affiliation></affiliation></author><author><name sortKey="Petricoin Iii, Emanuel F" sort="Petricoin Iii, Emanuel F" uniqKey="Petricoin Iii E" first="Emanuel F." last="Petricoin Iii">Emanuel F. Petricoin Iii</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, 800 Rockville Pike, Building 29A, Room 2A 17, Bethesda, MD 20892, USA +1‐301‐480‐3256===</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:88529F567434F379288B348301A6C18FDDD060E0</idno><date when="2004" year="2004">2004</date><idno type="doi">10.1002/pmic.200300573</idno><idno type="url">https://api.istex.fr/document/88529F567434F379288B348301A6C18FDDD060E0/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">004036</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">004036</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Proteomic analysis of lymph</title><author><name sortKey="Leak, Lee V" sort="Leak, Lee V" uniqKey="Leak L" first="Lee V." last="Leak">Lee V. Leak</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Ernest E. Just Laboratory of Cellular Biology, College of Medicine, Howard University, Washington, DC, USA</mods:affiliation></affiliation></author><author><name sortKey="Liotta, Lance A" sort="Liotta, Lance A" uniqKey="Liotta L" first="Lance A." last="Liotta">Lance A. Liotta</name><affiliation><mods:affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Krutzsch, Henry" sort="Krutzsch, Henry" uniqKey="Krutzsch H" first="Henry" last="Krutzsch">Henry Krutzsch</name><affiliation><mods:affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Jones, Michael" sort="Jones, Michael" uniqKey="Jones M" first="Michael" last="Jones">Michael Jones</name><affiliation><mods:affiliation>Laboratory of Animal Surgery, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Fusaroa, Vincent A" sort="Fusaroa, Vincent A" uniqKey="Fusaroa V" first="Vincent A." last="Fusaroa">Vincent A. Fusaroa</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Ross, Sally J" sort="Ross, Sally J" uniqKey="Ross S" first="Sally J." last="Ross">Sally J. Ross</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation></author><author><name sortKey="Zhao, Yingming" sort="Zhao, Yingming" uniqKey="Zhao Y" first="Yingming" last="Zhao">Yingming Zhao</name><affiliation><mods:affiliation>Department of Biochemistry, U. T. Southwestern Medical Center, Dallas, TX, USA</mods:affiliation></affiliation></author><author><name sortKey="Petricoin Iii, Emanuel F" sort="Petricoin Iii, Emanuel F" uniqKey="Petricoin Iii E" first="Emanuel F." last="Petricoin Iii">Emanuel F. Petricoin Iii</name><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</mods:affiliation></affiliation><affiliation><mods:affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, 800 Rockville Pike, Building 29A, Room 2A 17, Bethesda, MD 20892, USA +1‐301‐480‐3256===</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">PROTEOMICS</title><title level="j" type="alt">PROTEOMICS</title><idno type="ISSN">1615-9853</idno><idno type="eISSN">1615-9861</idno><imprint><biblScope unit="vol">4</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="753">753</biblScope><biblScope unit="page" to="765">765</biblScope><biblScope unit="page-count">13</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2004-03">2004-03</date></imprint><idno type="ISSN">1615-9853</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1615-9853</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">This report provides the first proteomic analysis of normal ovine lymph. By establishing the fact that lymph is more than an ultrafiltrate of blood plasma, it documents that the lymph proteome contains an array of proteins that differentiates it from plasma. The protein chip technology, surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry (SELDI‐TOF‐MS), two‐dimensional gel electrophoresis (2‐D PAGE) and MS, were employed to examine the protein expression profiles of ovine lymph. Using a weak cation exchange chip surface to assay lymph and plasma samples by SELDI‐TOF‐MS showed that the analysis of peak maps from lymph contained three protein peaks that were found only in lymph, while analysis of peak maps from plasma samples showed that five protein peaks were found only in plasma. Lymph and plasma samples showed eight peaks that were common to both. There were also more ions present in plasma than in lymph, which is consistent with the 2‐D PAGE analysis. MS analysis of a large number of protein spots from 2‐D PAGE gels of lymph produced MS/MS sequences for 18 proteins that were identified by searching against a comprehensive protein sequence database. As in plasma, large protein spots of albumin dominated the protein pattern in lymph. Other major proteins identified in 2‐D PAGE gels of lymph included, fibrinogen α‐ and β‐chains, immunoglobulin G (IgG) heavy chain, serotransferrin precursor, lactoferrin, and apolipoprotein A‐1. Two proteins that were identified and were differentially expressed in lymph were glial fibrillary astrocyte acidic protein and neutrophil cytosol factor‐1. By bringing the technologies of proteomics to bear on the analysis of lymph, it is possible to detect proteins in lymph that are quantitatively and qualitatively differentially expressed from those of plasma.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>lymph</json:string><json:string>protein spots</json:string><json:string>proteomics</json:string><json:string>lymphatic</json:string><json:string>fibrinogen</json:string><json:string>tauras</json:string><json:string>gmbh</json:string><json:string>proteomic</json:string><json:string>kgaa</json:string><json:string>proteome</json:string><json:string>verlag gmbh</json:string><json:string>weinheim</json:string><json:string>verlag</json:string><json:string>ovine</json:string><json:string>database</json:string><json:string>plasma samples</json:string><json:string>peptide</json:string><json:string>acidic</json:string><json:string>lymph samples</json:string><json:string>glial</json:string><json:string>peak maps</json:string><json:string>neutrophil</json:string><json:string>tryptic</json:string><json:string>coomassie</json:string><json:string>lymph proteins</json:string><json:string>seldi</json:string><json:string>lymphatic endothelium</json:string><json:string>protein peaks</json:string><json:string>plasma proteins</json:string><json:string>protein fingerprint</json:string><json:string>large number</json:string><json:string>protein expression profiles</json:string><json:string>lymph proteome</json:string><json:string>protein</json:string><json:string>blood plasma</json:string><json:string>weinheim proteomics</json:string><json:string>ovine lymph</json:string><json:string>normal ovine lymph</json:string><json:string>lymphatic system</json:string><json:string>glial fibrillary astrocyte acidic protein</json:string><json:string>page analysis</json:string><json:string>mass spectrometry</json:string><json:string>protein chip technology</json:string><json:string>protein spot resolution</json:string><json:string>corresponding page</json:string><json:string>laldieiatyr glial acidic protein</json:string><json:string>protein pattern</json:string><json:string>neutrophil nadph oxidase</json:string><json:string>weak cation exchange</json:string><json:string>serotransferrin precursor</json:string><json:string>silver staining</json:string><json:string>protein spot</json:string><json:string>national institutes</json:string><json:string>tryptic digestion</json:string><json:string>neutrophil cytosol</json:string><json:string>proteomic analysis</json:string><json:string>body fluids</json:string><json:string>plasma</json:string><json:string>leak</json:string><json:string>lower intensities</json:string><json:string>specific differences</json:string><json:string>molecular weight classes</json:string><json:string>lymphatic vessels</json:string><json:string>large amounts</json:string><json:string>systemic circulation</json:string><json:string>connective tissue cells</json:string><json:string>metabolic products</json:string><json:string>heavy chain</json:string><json:string>protein chip</json:string><json:string>chip surface</json:string><json:string>large protein spots</json:string><json:string>global view</json:string><json:string>protein expression</json:string><json:string>acetic acid</json:string><json:string>deionized water</json:string><json:string>sypro ruby protein</json:string><json:string>proteins spots</json:string><json:string>comprehensive protein sequence database</json:string><json:string>more ions</json:string><json:string>tryptic peptides</json:string><json:string>human plasma page</json:string><json:string>seldi technology</json:string><json:string>prominent protein peaks</json:string><json:string>complex mixtures</json:string><json:string>protein peak maps</json:string><json:string>silverstained page</json:string><json:string>electrophoresis page</json:string><json:string>protein alterations</json:string><json:string>individual protein spots</json:string><json:string>protein components</json:string><json:string>blood institute</json:string><json:string>lymph sample</json:string><json:string>different protein spots</json:string><json:string>national cancer institute</json:string><json:string>drug administration</json:string><json:string>therapeutic proteins</json:string><json:string>clinical proteomics program</json:string><json:string>agqdvaqaksqiksr neutrophil cytosol factor1</json:string><json:string>amino acid sequence</json:string><json:string>page access</json:string><json:string>present study</json:string><json:string>pathological states</json:string><json:string>filamentous components</json:string><json:string>elastic fibers</json:string><json:string>enzymatic components</json:string><json:string>normal lymph</json:string><json:string>specific proteins</json:string><json:string>cell biol</json:string><json:string>electrophoresis</json:string></teeft></keywords><author><json:item><name>Lee V. Leak</name><affiliations><json:string>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</json:string><json:string>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</json:string><json:string>Ernest E. Just Laboratory of Cellular Biology, College of Medicine, Howard University, Washington, DC, USA</json:string></affiliations></json:item><json:item><name>Lance A. Liotta</name><affiliations><json:string>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</json:string></affiliations></json:item><json:item><name>Henry Krutzsch</name><affiliations><json:string>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</json:string></affiliations></json:item><json:item><name>Michael Jones</name><affiliations><json:string>Laboratory of Animal Surgery, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA</json:string></affiliations></json:item><json:item><name>Vincent A. Fusaroa</name><affiliations><json:string>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</json:string></affiliations></json:item><json:item><name>Sally J. Ross</name><affiliations><json:string>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</json:string></affiliations></json:item><json:item><name>Yingming Zhao</name><affiliations><json:string>Department of Biochemistry, U. T. Southwestern Medical Center, Dallas, TX, USA</json:string></affiliations></json:item><json:item><name>Emanuel F. Petricoin III</name><affiliations><json:string>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</json:string><json:string>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, 800 Rockville Pike, Building 29A, Room 2A 17, Bethesda, MD 20892, USA +1‐301‐480‐3256===</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Biomarkers</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Cancer</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lymph</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry</value></json:item></subject><articleId><json:string>PMIC200300573</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>This report provides the first proteomic analysis of normal ovine lymph. By establishing the fact that lymph is more than an ultrafiltrate of blood plasma, it documents that the lymph proteome contains an array of proteins that differentiates it from plasma. The protein chip technology, surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry (SELDI‐TOF‐MS), two‐dimensional gel electrophoresis (2‐D PAGE) and MS, were employed to examine the protein expression profiles of ovine lymph. Using a weak cation exchange chip surface to assay lymph and plasma samples by SELDI‐TOF‐MS showed that the analysis of peak maps from lymph contained three protein peaks that were found only in lymph, while analysis of peak maps from plasma samples showed that five protein peaks were found only in plasma. Lymph and plasma samples showed eight peaks that were common to both. There were also more ions present in plasma than in lymph, which is consistent with the 2‐D PAGE analysis. MS analysis of a large number of protein spots from 2‐D PAGE gels of lymph produced MS/MS sequences for 18 proteins that were identified by searching against a comprehensive protein sequence database. As in plasma, large protein spots of albumin dominated the protein pattern in lymph. Other major proteins identified in 2‐D PAGE gels of lymph included, fibrinogen α‐ and β‐chains, immunoglobulin G (IgG) heavy chain, serotransferrin precursor, lactoferrin, and apolipoprotein A‐1. Two proteins that were identified and were differentially expressed in lymph were glial fibrillary astrocyte acidic protein and neutrophil cytosol factor‐1. By bringing the technologies of proteomics to bear on the analysis of lymph, it is possible to detect proteins in lymph that are quantitatively and qualitatively differentially expressed from those of plasma.</abstract><qualityIndicators><score>8</score><pdfVersion>1.2</pdfVersion><pdfPageSize>595 x 842 pts (A4)</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>1842</abstractCharCount><pdfWordCount>6923</pdfWordCount><pdfCharCount>44090</pdfCharCount><pdfPageCount>13</pdfPageCount><abstractWordCount>278</abstractWordCount></qualityIndicators><title>Proteomic analysis of lymph</title><genre><json:string>article</json:string></genre><host><title>PROTEOMICS</title><language><json:string>unknown</json:string></language><doi><json:string>10.1002/(ISSN)1615-9861</json:string></doi><issn><json:string>1615-9853</json:string></issn><eissn><json:string>1615-9861</json:string></eissn><publisherId><json:string>PMIC</json:string></publisherId><volume>4</volume><issue>3</issue><pages><first>753</first><last>765</last><total>13</total></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Research Article</value></json:item></subject></host><categories><wos><json:string>science</json:string><json:string>biochemistry & molecular biology</json:string><json:string>biochemical research methods</json:string></wos><scienceMetrix><json:string>health sciences</json:string><json:string>biomedical research</json:string><json:string>biochemistry & molecular biology</json:string></scienceMetrix><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences medicales</json:string></inist></categories><publicationDate>2004</publicationDate><copyrightDate>2004</copyrightDate><doi><json:string>10.1002/pmic.200300573</json:string></doi><id>88529F567434F379288B348301A6C18FDDD060E0</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/88529F567434F379288B348301A6C18FDDD060E0/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/88529F567434F379288B348301A6C18FDDD060E0/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/88529F567434F379288B348301A6C18FDDD060E0/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Proteomic analysis of lymph</title></titleStmt><publicationStmt><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><availability><licence>Copyright © 2004 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</licence></availability><date type="published" when="2004-03"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main" xml:lang="en">Proteomic analysis of lymph</title><author xml:id="author-0000"><persName><forename type="first">Lee V.</forename><surname>Leak</surname></persName><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA<address><country key="US"></country></address></affiliation><affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA<address><country key="US"></country></address></affiliation><affiliation>Ernest E. Just Laboratory of Cellular Biology, College of Medicine, Howard University, Washington, DC, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">Lance A.</forename><surname>Liotta</surname></persName><affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">Henry</forename><surname>Krutzsch</surname></persName><affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Michael</forename><surname>Jones</surname></persName><affiliation>Laboratory of Animal Surgery, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Vincent A.</forename><surname>Fusaroa</surname></persName><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0005"><persName><forename type="first">Sally J.</forename><surname>Ross</surname></persName><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0006"><persName><forename type="first">Yingming</forename><surname>Zhao</surname></persName><affiliation>Department of Biochemistry, U. T. Southwestern Medical Center, Dallas, TX, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0007" role="corresp"><persName><genName>III</genName><forename type="first">Emanuel F.</forename><surname>Petricoin</surname></persName><email>petricoin@cber.fda.gov</email><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA<address><country key="US"></country></address></affiliation><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, 800 Rockville Pike, Building 29A, Room 2A 17, Bethesda, MD 20892, USA Fax: +1‐301‐480‐3256===</affiliation></author><idno type="istex">88529F567434F379288B348301A6C18FDDD060E0</idno><idno type="DOI">10.1002/pmic.200300573</idno><idno type="unit">PMIC200300573</idno><idno type="toTypesetVersion">file:PMIC.PMIC200300573.pdf</idno></analytic><monogr><title level="j" type="main">PROTEOMICS</title><title level="j" type="alt">PROTEOMICS</title><idno type="pISSN">1615-9853</idno><idno type="eISSN">1615-9861</idno><idno type="book-DOI">10.1002/(ISSN)1615-9861</idno><idno type="book-part-DOI">10.1002/pmic.v4:3</idno><idno type="product">PMIC</idno><imprint><biblScope unit="vol">4</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="753">753</biblScope><biblScope unit="page" to="765">765</biblScope><biblScope unit="page-count">13</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2004-03"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>This report provides the first proteomic analysis of normal ovine lymph. By establishing the fact that lymph is more than an ultrafiltrate of blood plasma, it documents that the lymph proteome contains an array of proteins that differentiates it from plasma. The protein chip technology, surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry (SELDI‐TOF‐MS), two‐dimensional gel electrophoresis (2‐D PAGE) and MS, were employed to examine the protein expression profiles of ovine lymph. Using a weak cation exchange chip surface to assay lymph and plasma samples by SELDI‐TOF‐MS showed that the analysis of peak maps from lymph contained three protein peaks that were found only in lymph, while analysis of peak maps from plasma samples showed that five protein peaks were found only in plasma. Lymph and plasma samples showed eight peaks that were common to both. There were also more ions present in plasma than in lymph, which is consistent with the 2‐D PAGE analysis. MS analysis of a large number of protein spots from 2‐D PAGE gels of lymph produced MS/MS sequences for 18 proteins that were identified by searching against a comprehensive protein sequence database. As in plasma, large protein spots of albumin dominated the protein pattern in lymph. Other major proteins identified in 2‐D PAGE gels of lymph included, fibrinogen α‐ and β‐chains, immunoglobulin G (IgG) heavy chain, serotransferrin precursor, lactoferrin, and apolipoprotein A‐1. Two proteins that were identified and were differentially expressed in lymph were glial fibrillary astrocyte acidic protein and neutrophil cytosol factor‐1. By bringing the technologies of proteomics to bear on the analysis of lymph, it is possible to detect proteins in lymph that are quantitatively and qualitatively differentially expressed from those of plasma.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="kwd1">Biomarkers</term><term xml:id="kwd2">Cancer</term><term xml:id="kwd3">Lymph</term><term xml:id="kwd4">Surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry</term></keywords><classCode scheme="articleCategory">Research Article</classCode></textClass><langUsage><language ident="EN"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/88529F567434F379288B348301A6C18FDDD060E0/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>WILEY‐VCH Verlag</publisherName><publisherLoc>Weinheim</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1615-9861</doi><issn type="print">1615-9853</issn><issn type="electronic">1615-9861</issn><idGroup><id type="product" value="PMIC"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="PROTEOMICS">PROTEOMICS</title><title type="short">Proteomics</title></titleGroup></publicationMeta><publicationMeta level="part" position="30"><doi origin="wiley" registered="yes">10.1002/pmic.v4:3</doi><numberingGroup><numbering type="journalVolume" number="4">4</numbering><numbering type="journalIssue">3</numbering></numberingGroup><coverDate startDate="2004-03">March 2004</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="21" status="forIssue"><doi origin="wiley" registered="yes">10.1002/pmic.200300573</doi><idGroup><id type="unit" value="PMIC200300573"></id></idGroup><countGroup><count type="pageTotal" number="13"></count></countGroup><titleGroup><title type="articleCategory">Research Article</title></titleGroup><copyright ownership="publisher">Copyright © 2004 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</copyright><eventGroup><event type="manuscriptReceived" date="2003-03-31"></event><event type="firstOnline" date="2003-09-17"></event><event type="publishedOnlineFinalForm" date="2004-02-19"></event><event type="publishedOnlineAcceptedOrEarlyUnpaginated" date="2003-09-17"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.5.2 mode:FullText source:HeaderRef result:HeaderRef" date="2011-07-06"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:4.0.1" date="2014-03-20"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-11-03"></event></eventGroup><numberingGroup><numbering type="pageFirst">753</numbering><numbering type="pageLast">765</numbering></numberingGroup><correspondenceTo>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, 800 Rockville Pike, Building 29A, Room 2A 17, Bethesda, MD 20892, USA <b>Fax:</b> +1‐301‐480‐3256===</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:PMIC.PMIC200300573.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="5"></count><count type="tableTotal" number="2"></count><count type="referenceTotal" number="50"></count></countGroup><titleGroup><title type="main" xml:lang="en">Proteomic analysis of lymph</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#a1 #a2 #a3"><personName><givenNames>Lee V.</givenNames><familyName>Leak</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#a2"><personName><givenNames>Lance A.</givenNames><familyName>Liotta</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#a2"><personName><givenNames>Henry</givenNames><familyName>Krutzsch</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#a4"><personName><givenNames>Michael</givenNames><familyName>Jones</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#a1"><personName><givenNames>Vincent A.</givenNames><familyName>Fusaroa</familyName></personName></creator><creator xml:id="au6" creatorRole="author" affiliationRef="#a1"><personName><givenNames>Sally J.</givenNames><familyName>Ross</familyName></personName></creator><creator xml:id="au7" creatorRole="author" affiliationRef="#a5"><personName><givenNames>Yingming</givenNames><familyName>Zhao</familyName></personName></creator><creator xml:id="au8" creatorRole="author" affiliationRef="#a1" corresponding="yes"><personName><givenNames>Emanuel F.</givenNames><familyName>Petricoin</familyName><nameSuffix>III</nameSuffix></personName><contactDetails><email>petricoin@cber.fda.gov</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="US" type="organization"><unparsedAffiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="US" type="organization"><unparsedAffiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</unparsedAffiliation></affiliation><affiliation xml:id="a3" countryCode="US" type="organization"><unparsedAffiliation>Ernest E. Just Laboratory of Cellular Biology, College of Medicine, Howard University, Washington, DC, USA</unparsedAffiliation></affiliation><affiliation xml:id="a4" countryCode="US" type="organization"><unparsedAffiliation>Laboratory of Animal Surgery, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA</unparsedAffiliation></affiliation><affiliation xml:id="a5" countryCode="US" type="organization"><unparsedAffiliation>Department of Biochemistry, U. T. Southwestern Medical Center, Dallas, TX, USA</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">Biomarkers</keyword><keyword xml:id="kwd2">Cancer</keyword><keyword xml:id="kwd3">Lymph</keyword><keyword xml:id="kwd4">Surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>This report provides the first proteomic analysis of normal ovine lymph. By establishing the fact that lymph is more than an ultrafiltrate of blood plasma, it documents that the lymph proteome contains an array of proteins that differentiates it from plasma. The protein chip technology, surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry (SELDI‐TOF‐MS), two‐dimensional gel electrophoresis (2‐D PAGE) and MS, were employed to examine the protein expression profiles of ovine lymph. Using a weak cation exchange chip surface to assay lymph and plasma samples by SELDI‐TOF‐MS showed that the analysis of peak maps from lymph contained three protein peaks that were found only in lymph, while analysis of peak maps from plasma samples showed that five protein peaks were found only in plasma. Lymph and plasma samples showed eight peaks that were common to both. There were also more ions present in plasma than in lymph, which is consistent with the 2‐D PAGE analysis. MS analysis of a large number of protein spots from 2‐D PAGE gels of lymph produced MS/MS sequences for 18 proteins that were identified by searching against a comprehensive protein sequence database. As in plasma, large protein spots of albumin dominated the protein pattern in lymph. Other major proteins identified in 2‐D PAGE gels of lymph included, fibrinogen α‐ and β‐chains, immunoglobulin G (IgG) heavy chain, serotransferrin precursor, lactoferrin, and apolipoprotein A‐1. Two proteins that were identified and were differentially expressed in lymph were glial fibrillary astrocyte acidic protein and neutrophil cytosol factor‐1. By bringing the technologies of proteomics to bear on the analysis of lymph, it is possible to detect proteins in lymph that are quantitatively and qualitatively differentially expressed from those of plasma.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Proteomic analysis of lymph</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Proteomic analysis of lymph</title></titleInfo><name type="personal"><namePart type="given">Lee V.</namePart><namePart type="family">Leak</namePart><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</affiliation><affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</affiliation><affiliation>Ernest E. Just Laboratory of Cellular Biology, College of Medicine, Howard University, Washington, DC, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Lance A.</namePart><namePart type="family">Liotta</namePart><affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Henry</namePart><namePart type="family">Krutzsch</namePart><affiliation>Laboratory of Pathology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michael</namePart><namePart type="family">Jones</namePart><affiliation>Laboratory of Animal Surgery, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Vincent A.</namePart><namePart type="family">Fusaroa</namePart><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sally J.</namePart><namePart type="family">Ross</namePart><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Yingming</namePart><namePart type="family">Zhao</namePart><affiliation>Department of Biochemistry, U. T. Southwestern Medical Center, Dallas, TX, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Emanuel F.</namePart><namePart type="family">Petricoin III</namePart><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, Bethesda, MD, USA</affiliation><affiliation>Clinical Proteomics Program of Therapeutic Proteins, CBER, Food and Drug Administration, 800 Rockville Pike, Building 29A, Room 2A 17, Bethesda, MD 20892, USA +1‐301‐480‐3256===</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>WILEY‐VCH Verlag</publisher><place><placeTerm type="text">Weinheim</placeTerm></place><dateIssued encoding="w3cdtf">2004-03</dateIssued><dateCaptured encoding="w3cdtf">2003-03-31</dateCaptured><copyrightDate encoding="w3cdtf">2004</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">5</extent><extent unit="tables">2</extent><extent unit="references">50</extent></physicalDescription><abstract lang="en">This report provides the first proteomic analysis of normal ovine lymph. By establishing the fact that lymph is more than an ultrafiltrate of blood plasma, it documents that the lymph proteome contains an array of proteins that differentiates it from plasma. The protein chip technology, surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry (SELDI‐TOF‐MS), two‐dimensional gel electrophoresis (2‐D PAGE) and MS, were employed to examine the protein expression profiles of ovine lymph. Using a weak cation exchange chip surface to assay lymph and plasma samples by SELDI‐TOF‐MS showed that the analysis of peak maps from lymph contained three protein peaks that were found only in lymph, while analysis of peak maps from plasma samples showed that five protein peaks were found only in plasma. Lymph and plasma samples showed eight peaks that were common to both. There were also more ions present in plasma than in lymph, which is consistent with the 2‐D PAGE analysis. MS analysis of a large number of protein spots from 2‐D PAGE gels of lymph produced MS/MS sequences for 18 proteins that were identified by searching against a comprehensive protein sequence database. As in plasma, large protein spots of albumin dominated the protein pattern in lymph. Other major proteins identified in 2‐D PAGE gels of lymph included, fibrinogen α‐ and β‐chains, immunoglobulin G (IgG) heavy chain, serotransferrin precursor, lactoferrin, and apolipoprotein A‐1. Two proteins that were identified and were differentially expressed in lymph were glial fibrillary astrocyte acidic protein and neutrophil cytosol factor‐1. By bringing the technologies of proteomics to bear on the analysis of lymph, it is possible to detect proteins in lymph that are quantitatively and qualitatively differentially expressed from those of plasma.</abstract><subject lang="en"><genre>keywords</genre><topic>Biomarkers</topic><topic>Cancer</topic><topic>Lymph</topic><topic>Surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry</topic></subject><relatedItem type="host"><titleInfo><title>PROTEOMICS</title></titleInfo><titleInfo type="abbreviated"><title>Proteomics</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Research Article</topic></subject><identifier type="ISSN">1615-9853</identifier><identifier type="eISSN">1615-9861</identifier><identifier type="DOI">10.1002/(ISSN)1615-9861</identifier><identifier type="PublisherID">PMIC</identifier><part><date>2004</date><detail type="volume"><caption>vol.</caption><number>4</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>753</start><end>765</end><total>13</total></extent></part></relatedItem><identifier type="istex">88529F567434F379288B348301A6C18FDDD060E0</identifier><identifier type="DOI">10.1002/pmic.200300573</identifier><identifier type="ArticleID">PMIC200300573</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 2004 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>WILEY‐VCH Verlag</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/LymphedemaV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 004036 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 004036 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= LymphedemaV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:88529F567434F379288B348301A6C18FDDD060E0
|texte= Proteomic analysis of lymph
}}
| This area was generated with Dilib version V0.6.31. |  |