Proteomic characterization of inter-alpha inhibitor proteins from human plasma
Inter‐alpha inhibitor proteins (IaIp) are a family of structurally related serine protease inhibitors found in relatively high concentrations in human plasma. Recent studies have implicated a role for IaIp in sepsis, and have demonstrated their potential as biomarkers in sepsis and cancer. For chara...
Gespeichert in:
Veröffentlicht in: | Proteomics (Weinheim) 2006-05, Vol.6 (9), p.2874-2885 |
---|---|
Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 2885 |
---|---|
container_issue | 9 |
container_start_page | 2874 |
container_title | Proteomics (Weinheim) |
container_volume | 6 |
creator | Josic, Djuro Brown, Mari Kino Huang, Feilei Lim, Yow-Pin Rucevic, Marijana Clifton, James G. Hixson, Douglas C. |
description | Inter‐alpha inhibitor proteins (IaIp) are a family of structurally related serine protease inhibitors found in relatively high concentrations in human plasma. Recent studies have implicated a role for IaIp in sepsis, and have demonstrated their potential as biomarkers in sepsis and cancer. For characterization of isolated IaI proteins and contaminating proteins during the last steps of the purification process, SELDI‐TOF MS and HPLC–ESI‐MS/MS were used. After separation by SDS‐PAGE or 2‐DE, polypeptide bands of 80, 125 and 250 kDa were excised from gels and digested by trypsin. The tryptic peptides were analyzed by both MS methods. The main contamination during the purification process, a band of 80 kDa, contains mainly IaIp heavy chain (HC) H3. HC H1 and H2 were also found in this band. In addition, some vitamin K‐dependent clotting factors and inhibitors and other plasma proteins were identified. The 125‐kDa band, representing the pre‐alpha inhibitor, was found to contain both bikunin and HC H3. The presence of other HC H1, H2 and the recently described HC H4 was also detected by SELDI‐TOF MS. The presence of HC H1, H2, and H3 in the 125‐kDa band was confirmed by ESI‐MS/MS, but not the presence of the H4. Three polypeptides, H1 and H2 together with bikunin, were identified in the 250‐kDa band, representing the ITI, by both MS techniques. Once again, the presence of H4 was detected in this band only by SELDI‐TOF MS, but the number of corresponding peptides was still not sufficient for final identification of this polypeptide. The importance of the application of proteomic methods for the proper evaluation of therapeutic drugs based on human plasma is discussed. |
doi_str_mv | 10.1002/pmic.200500563 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67949478</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>67949478</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5083-ca9b37b6c67fa10cfb9a4569495307164cbb3be35f0c929fd89be03c73faa383</originalsourceid><addsrcrecordid>eNqFkEtLAzEURoMovrcuZTa6m5o0k2SylPEJ9QEKLsNNTGh0XiZTtP56U1qqOyGQGzjfl8tB6IjgEcF4fNY33ozGGLN0ON1Au4QTlsuSk831zOgO2ovxDWMiSim20Q7hTHKB-S66fwzdYLvUkpkpBDCDDf4bBt-1Wecy36Z3DnU_hTRPvfZDF7J-kfFtzFzommw6a6DN-hpiAwdoy0Ed7eHq3kfPV5fP1U0-ebi-rc4nuWG4pLkBqanQ3HDhgGDjtISCcVlIRrEgvDBaU20pc9jIsXSvpdQWUyOoA6Al3Ueny9q0ycfMxkE1Phpb19DabhYVF6mqEP-DRBaMEiISOFqCJnQxButUH3wDYa4IVgvTamFarU2nwPGqeaYb-_qLr9Qm4GQFQDRQuwCt8fGXE6KQhOLEySX36Ws7_-db9Xh3W_1dIl9mfRzs1zoL4T0poIKpl_tr9VQ9XUwortSY_gAV0qeL</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19453117</pqid></control><display><type>article</type><title>Proteomic characterization of inter-alpha inhibitor proteins from human plasma</title><source>MEDLINE</source><source>Wiley Online Library All Journals</source><creator>Josic, Djuro ; Brown, Mari Kino ; Huang, Feilei ; Lim, Yow-Pin ; Rucevic, Marijana ; Clifton, James G. ; Hixson, Douglas C.</creator><creatorcontrib>Josic, Djuro ; Brown, Mari Kino ; Huang, Feilei ; Lim, Yow-Pin ; Rucevic, Marijana ; Clifton, James G. ; Hixson, Douglas C.</creatorcontrib><description>Inter‐alpha inhibitor proteins (IaIp) are a family of structurally related serine protease inhibitors found in relatively high concentrations in human plasma. Recent studies have implicated a role for IaIp in sepsis, and have demonstrated their potential as biomarkers in sepsis and cancer. For characterization of isolated IaI proteins and contaminating proteins during the last steps of the purification process, SELDI‐TOF MS and HPLC–ESI‐MS/MS were used. After separation by SDS‐PAGE or 2‐DE, polypeptide bands of 80, 125 and 250 kDa were excised from gels and digested by trypsin. The tryptic peptides were analyzed by both MS methods. The main contamination during the purification process, a band of 80 kDa, contains mainly IaIp heavy chain (HC) H3. HC H1 and H2 were also found in this band. In addition, some vitamin K‐dependent clotting factors and inhibitors and other plasma proteins were identified. The 125‐kDa band, representing the pre‐alpha inhibitor, was found to contain both bikunin and HC H3. The presence of other HC H1, H2 and the recently described HC H4 was also detected by SELDI‐TOF MS. The presence of HC H1, H2, and H3 in the 125‐kDa band was confirmed by ESI‐MS/MS, but not the presence of the H4. Three polypeptides, H1 and H2 together with bikunin, were identified in the 250‐kDa band, representing the ITI, by both MS techniques. Once again, the presence of H4 was detected in this band only by SELDI‐TOF MS, but the number of corresponding peptides was still not sufficient for final identification of this polypeptide. The importance of the application of proteomic methods for the proper evaluation of therapeutic drugs based on human plasma is discussed.</description><identifier>ISSN: 1615-9853</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.200500563</identifier><identifier>PMID: 16596706</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Alpha-Globulins - analysis ; Alpha-Globulins - isolation & purification ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Biomarkers ; Diagnostic and therapeutic agents ; Fundamental and applied biological sciences. Psychology ; Gas Chromatography-Mass Spectrometry ; Humans ; Inter-alpha inhibitor proteins ; Membrane Glycoproteins - blood ; Membrane Glycoproteins - isolation & purification ; Miscellaneous ; Molecular Sequence Data ; Plasma - chemistry ; Proteins ; Proteomic characterization ; Proteomics ; Serine Proteinase Inhibitors - blood ; Serine Proteinase Inhibitors - isolation & purification ; Spectrometry, Mass, Electrospray Ionization ; Trypsin Inhibitor, Kunitz Soybean - blood ; Trypsin Inhibitor, Kunitz Soybean - isolation & purification</subject><ispartof>Proteomics (Weinheim), 2006-05, Vol.6 (9), p.2874-2885</ispartof><rights>Copyright © 2006 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5083-ca9b37b6c67fa10cfb9a4569495307164cbb3be35f0c929fd89be03c73faa383</citedby><cites>FETCH-LOGICAL-c5083-ca9b37b6c67fa10cfb9a4569495307164cbb3be35f0c929fd89be03c73faa383</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fpmic.200500563$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fpmic.200500563$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17749130$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16596706$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Josic, Djuro</creatorcontrib><creatorcontrib>Brown, Mari Kino</creatorcontrib><creatorcontrib>Huang, Feilei</creatorcontrib><creatorcontrib>Lim, Yow-Pin</creatorcontrib><creatorcontrib>Rucevic, Marijana</creatorcontrib><creatorcontrib>Clifton, James G.</creatorcontrib><creatorcontrib>Hixson, Douglas C.</creatorcontrib><title>Proteomic characterization of inter-alpha inhibitor proteins from human plasma</title><title>Proteomics (Weinheim)</title><addtitle>Proteomics</addtitle><description>Inter‐alpha inhibitor proteins (IaIp) are a family of structurally related serine protease inhibitors found in relatively high concentrations in human plasma. Recent studies have implicated a role for IaIp in sepsis, and have demonstrated their potential as biomarkers in sepsis and cancer. For characterization of isolated IaI proteins and contaminating proteins during the last steps of the purification process, SELDI‐TOF MS and HPLC–ESI‐MS/MS were used. After separation by SDS‐PAGE or 2‐DE, polypeptide bands of 80, 125 and 250 kDa were excised from gels and digested by trypsin. The tryptic peptides were analyzed by both MS methods. The main contamination during the purification process, a band of 80 kDa, contains mainly IaIp heavy chain (HC) H3. HC H1 and H2 were also found in this band. In addition, some vitamin K‐dependent clotting factors and inhibitors and other plasma proteins were identified. The 125‐kDa band, representing the pre‐alpha inhibitor, was found to contain both bikunin and HC H3. The presence of other HC H1, H2 and the recently described HC H4 was also detected by SELDI‐TOF MS. The presence of HC H1, H2, and H3 in the 125‐kDa band was confirmed by ESI‐MS/MS, but not the presence of the H4. Three polypeptides, H1 and H2 together with bikunin, were identified in the 250‐kDa band, representing the ITI, by both MS techniques. Once again, the presence of H4 was detected in this band only by SELDI‐TOF MS, but the number of corresponding peptides was still not sufficient for final identification of this polypeptide. The importance of the application of proteomic methods for the proper evaluation of therapeutic drugs based on human plasma is discussed.</description><subject>Alpha-Globulins - analysis</subject><subject>Alpha-Globulins - isolation & purification</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomarkers</subject><subject>Diagnostic and therapeutic agents</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gas Chromatography-Mass Spectrometry</subject><subject>Humans</subject><subject>Inter-alpha inhibitor proteins</subject><subject>Membrane Glycoproteins - blood</subject><subject>Membrane Glycoproteins - isolation & purification</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Plasma - chemistry</subject><subject>Proteins</subject><subject>Proteomic characterization</subject><subject>Proteomics</subject><subject>Serine Proteinase Inhibitors - blood</subject><subject>Serine Proteinase Inhibitors - isolation & purification</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><subject>Trypsin Inhibitor, Kunitz Soybean - blood</subject><subject>Trypsin Inhibitor, Kunitz Soybean - isolation & purification</subject><issn>1615-9853</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLAzEURoMovrcuZTa6m5o0k2SylPEJ9QEKLsNNTGh0XiZTtP56U1qqOyGQGzjfl8tB6IjgEcF4fNY33ozGGLN0ON1Au4QTlsuSk831zOgO2ovxDWMiSim20Q7hTHKB-S66fwzdYLvUkpkpBDCDDf4bBt-1Wecy36Z3DnU_hTRPvfZDF7J-kfFtzFzommw6a6DN-hpiAwdoy0Ed7eHq3kfPV5fP1U0-ebi-rc4nuWG4pLkBqanQ3HDhgGDjtISCcVlIRrEgvDBaU20pc9jIsXSvpdQWUyOoA6Al3Ueny9q0ycfMxkE1Phpb19DabhYVF6mqEP-DRBaMEiISOFqCJnQxButUH3wDYa4IVgvTamFarU2nwPGqeaYb-_qLr9Qm4GQFQDRQuwCt8fGXE6KQhOLEySX36Ws7_-db9Xh3W_1dIl9mfRzs1zoL4T0poIKpl_tr9VQ9XUwortSY_gAV0qeL</recordid><startdate>20060501</startdate><enddate>20060501</enddate><creator>Josic, Djuro</creator><creator>Brown, Mari Kino</creator><creator>Huang, Feilei</creator><creator>Lim, Yow-Pin</creator><creator>Rucevic, Marijana</creator><creator>Clifton, James G.</creator><creator>Hixson, Douglas C.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley-VCH</general><scope>BSCLL</scope><scope>IQODW</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>7QL</scope><scope>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20060501</creationdate><title>Proteomic characterization of inter-alpha inhibitor proteins from human plasma</title><author>Josic, Djuro ; Brown, Mari Kino ; Huang, Feilei ; Lim, Yow-Pin ; Rucevic, Marijana ; Clifton, James G. ; Hixson, Douglas C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5083-ca9b37b6c67fa10cfb9a4569495307164cbb3be35f0c929fd89be03c73faa383</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Alpha-Globulins - analysis</topic><topic>Alpha-Globulins - isolation & purification</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biomarkers</topic><topic>Diagnostic and therapeutic agents</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gas Chromatography-Mass Spectrometry</topic><topic>Humans</topic><topic>Inter-alpha inhibitor proteins</topic><topic>Membrane Glycoproteins - blood</topic><topic>Membrane Glycoproteins - isolation & purification</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Plasma - chemistry</topic><topic>Proteins</topic><topic>Proteomic characterization</topic><topic>Proteomics</topic><topic>Serine Proteinase Inhibitors - blood</topic><topic>Serine Proteinase Inhibitors - isolation & purification</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><topic>Trypsin Inhibitor, Kunitz Soybean - blood</topic><topic>Trypsin Inhibitor, Kunitz Soybean - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Josic, Djuro</creatorcontrib><creatorcontrib>Brown, Mari Kino</creatorcontrib><creatorcontrib>Huang, Feilei</creatorcontrib><creatorcontrib>Lim, Yow-Pin</creatorcontrib><creatorcontrib>Rucevic, Marijana</creatorcontrib><creatorcontrib>Clifton, James G.</creatorcontrib><creatorcontrib>Hixson, Douglas C.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Proteomics (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Josic, Djuro</au><au>Brown, Mari Kino</au><au>Huang, Feilei</au><au>Lim, Yow-Pin</au><au>Rucevic, Marijana</au><au>Clifton, James G.</au><au>Hixson, Douglas C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteomic characterization of inter-alpha inhibitor proteins from human plasma</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2006-05-01</date><risdate>2006</risdate><volume>6</volume><issue>9</issue><spage>2874</spage><epage>2885</epage><pages>2874-2885</pages><issn>1615-9853</issn><eissn>1615-9861</eissn><abstract>Inter‐alpha inhibitor proteins (IaIp) are a family of structurally related serine protease inhibitors found in relatively high concentrations in human plasma. Recent studies have implicated a role for IaIp in sepsis, and have demonstrated their potential as biomarkers in sepsis and cancer. For characterization of isolated IaI proteins and contaminating proteins during the last steps of the purification process, SELDI‐TOF MS and HPLC–ESI‐MS/MS were used. After separation by SDS‐PAGE or 2‐DE, polypeptide bands of 80, 125 and 250 kDa were excised from gels and digested by trypsin. The tryptic peptides were analyzed by both MS methods. The main contamination during the purification process, a band of 80 kDa, contains mainly IaIp heavy chain (HC) H3. HC H1 and H2 were also found in this band. In addition, some vitamin K‐dependent clotting factors and inhibitors and other plasma proteins were identified. The 125‐kDa band, representing the pre‐alpha inhibitor, was found to contain both bikunin and HC H3. The presence of other HC H1, H2 and the recently described HC H4 was also detected by SELDI‐TOF MS. The presence of HC H1, H2, and H3 in the 125‐kDa band was confirmed by ESI‐MS/MS, but not the presence of the H4. Three polypeptides, H1 and H2 together with bikunin, were identified in the 250‐kDa band, representing the ITI, by both MS techniques. Once again, the presence of H4 was detected in this band only by SELDI‐TOF MS, but the number of corresponding peptides was still not sufficient for final identification of this polypeptide. The importance of the application of proteomic methods for the proper evaluation of therapeutic drugs based on human plasma is discussed.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>16596706</pmid><doi>10.1002/pmic.200500563</doi><tpages>12</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1615-9853 |
ispartof | Proteomics (Weinheim), 2006-05, Vol.6 (9), p.2874-2885 |
issn | 1615-9853 1615-9861 |
language | eng |
recordid | cdi_proquest_miscellaneous_67949478 |
source | MEDLINE; Wiley Online Library All Journals |
subjects | Alpha-Globulins - analysis Alpha-Globulins - isolation & purification Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Biomarkers Diagnostic and therapeutic agents Fundamental and applied biological sciences. Psychology Gas Chromatography-Mass Spectrometry Humans Inter-alpha inhibitor proteins Membrane Glycoproteins - blood Membrane Glycoproteins - isolation & purification Miscellaneous Molecular Sequence Data Plasma - chemistry Proteins Proteomic characterization Proteomics Serine Proteinase Inhibitors - blood Serine Proteinase Inhibitors - isolation & purification Spectrometry, Mass, Electrospray Ionization Trypsin Inhibitor, Kunitz Soybean - blood Trypsin Inhibitor, Kunitz Soybean - isolation & purification |
title | Proteomic characterization of inter-alpha inhibitor proteins from human plasma |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T03%3A10%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Proteomic%20characterization%20of%20inter-alpha%20inhibitor%20proteins%20from%20human%20plasma&rft.jtitle=Proteomics%20(Weinheim)&rft.au=Josic,%20Djuro&rft.date=2006-05-01&rft.volume=6&rft.issue=9&rft.spage=2874&rft.epage=2885&rft.pages=2874-2885&rft.issn=1615-9853&rft.eissn=1615-9861&rft_id=info:doi/10.1002/pmic.200500563&rft_dat=%3Cproquest_cross%3E67949478%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19453117&rft_id=info:pmid/16596706&rfr_iscdi=true |