The Peripheral Blood Eosinophil Proteome
A system-wide understanding of biological processes requires a comprehensive knowledge of the proteins in the biological system. The eosinophil is a type of granulocytic leukocyte specified early in hematopoietic differentiation that participates in barrier defense, innate immunity, and allergic dis...
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Veröffentlicht in: | Journal of proteome research 2016-05, Vol.15 (5), p.1524-1533 |
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creator | Wilkerson, Emily M Johansson, Mats W Hebert, Alexander S Westphall, Michael S Mathur, Sameer K Jarjour, Nizar N Schwantes, Elizabeth A Mosher, Deane F Coon, Joshua J |
description | A system-wide understanding of biological processes requires a comprehensive knowledge of the proteins in the biological system. The eosinophil is a type of granulocytic leukocyte specified early in hematopoietic differentiation that participates in barrier defense, innate immunity, and allergic disease. The proteome of the eosinophil is largely unannotated with under 500 proteins identified. We now report a map of the nonstimulated peripheral blood eosinophil proteome assembled using two-dimensional liquid chromatography coupled with high-resolution mass spectrometry. Our analysis yielded 100,892 unique peptides mapping to 7,086 protein groups representing 6,813 genes as well as 4,802 site-specific phosphorylation events. We account for the contribution of platelets that routinely contaminate purified eosinophils and report the variability in the eosinophil proteome among five individuals and proteomic changes accompanying acute activation of eosinophils by interleukin-5. Our deep coverage and quantitative analyses fill an important gap in the existing maps of the human proteome and will enable the strategic use of proteomics to study eosinophils in human diseases. |
doi_str_mv | 10.1021/acs.jproteome.6b00006 |
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The eosinophil is a type of granulocytic leukocyte specified early in hematopoietic differentiation that participates in barrier defense, innate immunity, and allergic disease. The proteome of the eosinophil is largely unannotated with under 500 proteins identified. We now report a map of the nonstimulated peripheral blood eosinophil proteome assembled using two-dimensional liquid chromatography coupled with high-resolution mass spectrometry. Our analysis yielded 100,892 unique peptides mapping to 7,086 protein groups representing 6,813 genes as well as 4,802 site-specific phosphorylation events. We account for the contribution of platelets that routinely contaminate purified eosinophils and report the variability in the eosinophil proteome among five individuals and proteomic changes accompanying acute activation of eosinophils by interleukin-5. 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Proteome Res</addtitle><description>A system-wide understanding of biological processes requires a comprehensive knowledge of the proteins in the biological system. The eosinophil is a type of granulocytic leukocyte specified early in hematopoietic differentiation that participates in barrier defense, innate immunity, and allergic disease. The proteome of the eosinophil is largely unannotated with under 500 proteins identified. We now report a map of the nonstimulated peripheral blood eosinophil proteome assembled using two-dimensional liquid chromatography coupled with high-resolution mass spectrometry. Our analysis yielded 100,892 unique peptides mapping to 7,086 protein groups representing 6,813 genes as well as 4,802 site-specific phosphorylation events. We account for the contribution of platelets that routinely contaminate purified eosinophils and report the variability in the eosinophil proteome among five individuals and proteomic changes accompanying acute activation of eosinophils by interleukin-5. Our deep coverage and quantitative analyses fill an important gap in the existing maps of the human proteome and will enable the strategic use of proteomics to study eosinophils in human diseases.</description><subject>Chromatography, Liquid - methods</subject><subject>Eosinophils - chemistry</subject><subject>Humans</subject><subject>Interleukin-5 - pharmacology</subject><subject>Mass Spectrometry - methods</subject><subject>Phosphorylation</subject><subject>Proteome - analysis</subject><subject>Proteomics - methods</subject><issn>1535-3893</issn><issn>1535-3907</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAURC0EoqXwCaAsu0nx284GCarykCrRRVlbTuKQVEkc7BSJv8elaQUr7sZX8szc0QHgGsEZghjd6szPNp2zvbGNmfEUhuEnYIwYYTFJoDg97DIhI3Dh_QZCxAQk52CEBYQsoXwMpuvSRCvjqq40TtfRQ21tHi2sr1rblVUdrYYTl-Cs0LU3V8M7AW-Pi_X8OV6-Pr3M75expoz0MSpISjFFRhJmBM-pTjFOUlFIwzOcIk05zwTJMxk6MoQTzAgmIqccZVhKQSbgbp_bbdPG5Jlp-9BLda5qtPtSVlfq709blerdfiqGMWYiCQHTIcDZj63xvWoqn5m61q2xW6-QkIJKKOVOyvbSzFnvnSmOZxBUO8oqUFZHymqgHHw3vzseXQesQYD2gh-_3bo2IPsn9BtSHIyL</recordid><startdate>20160506</startdate><enddate>20160506</enddate><creator>Wilkerson, Emily M</creator><creator>Johansson, Mats W</creator><creator>Hebert, Alexander S</creator><creator>Westphall, Michael S</creator><creator>Mathur, Sameer K</creator><creator>Jarjour, Nizar N</creator><creator>Schwantes, Elizabeth A</creator><creator>Mosher, Deane F</creator><creator>Coon, Joshua J</creator><general>American Chemical Society</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>20160506</creationdate><title>The Peripheral Blood Eosinophil Proteome</title><author>Wilkerson, Emily M ; Johansson, Mats W ; Hebert, Alexander S ; Westphall, Michael S ; Mathur, Sameer K ; Jarjour, Nizar N ; Schwantes, Elizabeth A ; Mosher, Deane F ; Coon, Joshua J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a453t-1f3b4241e835e76d4ab229b7f8e6c2b1a466c73dc83905129253237d461c28873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Chromatography, Liquid - methods</topic><topic>Eosinophils - chemistry</topic><topic>Humans</topic><topic>Interleukin-5 - pharmacology</topic><topic>Mass Spectrometry - methods</topic><topic>Phosphorylation</topic><topic>Proteome - analysis</topic><topic>Proteomics - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilkerson, Emily M</creatorcontrib><creatorcontrib>Johansson, Mats W</creatorcontrib><creatorcontrib>Hebert, Alexander S</creatorcontrib><creatorcontrib>Westphall, Michael S</creatorcontrib><creatorcontrib>Mathur, Sameer K</creatorcontrib><creatorcontrib>Jarjour, Nizar N</creatorcontrib><creatorcontrib>Schwantes, Elizabeth A</creatorcontrib><creatorcontrib>Mosher, Deane F</creatorcontrib><creatorcontrib>Coon, Joshua J</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>Journal of proteome research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilkerson, Emily M</au><au>Johansson, Mats W</au><au>Hebert, Alexander S</au><au>Westphall, Michael S</au><au>Mathur, Sameer K</au><au>Jarjour, Nizar N</au><au>Schwantes, Elizabeth A</au><au>Mosher, Deane F</au><au>Coon, Joshua J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Peripheral Blood Eosinophil Proteome</atitle><jtitle>Journal of proteome research</jtitle><addtitle>J. Proteome Res</addtitle><date>2016-05-06</date><risdate>2016</risdate><volume>15</volume><issue>5</issue><spage>1524</spage><epage>1533</epage><pages>1524-1533</pages><issn>1535-3893</issn><eissn>1535-3907</eissn><abstract>A system-wide understanding of biological processes requires a comprehensive knowledge of the proteins in the biological system. The eosinophil is a type of granulocytic leukocyte specified early in hematopoietic differentiation that participates in barrier defense, innate immunity, and allergic disease. The proteome of the eosinophil is largely unannotated with under 500 proteins identified. We now report a map of the nonstimulated peripheral blood eosinophil proteome assembled using two-dimensional liquid chromatography coupled with high-resolution mass spectrometry. Our analysis yielded 100,892 unique peptides mapping to 7,086 protein groups representing 6,813 genes as well as 4,802 site-specific phosphorylation events. We account for the contribution of platelets that routinely contaminate purified eosinophils and report the variability in the eosinophil proteome among five individuals and proteomic changes accompanying acute activation of eosinophils by interleukin-5. Our deep coverage and quantitative analyses fill an important gap in the existing maps of the human proteome and will enable the strategic use of proteomics to study eosinophils in human diseases.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>27005946</pmid><doi>10.1021/acs.jproteome.6b00006</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Chromatography, Liquid - methods Eosinophils - chemistry Humans Interleukin-5 - pharmacology Mass Spectrometry - methods Phosphorylation Proteome - analysis Proteomics - methods |
title | The Peripheral Blood Eosinophil Proteome |
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