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Comparative Proteomics Reveal Diverse Functions and Dynamic Changes of Bombyx mori Silk Proteins Spun from Different Development Stages
Silkworms (Bombyx mori) produce massive amounts of silk proteins to make cocoons during the final stages of larval development. Although the major components, fibroin and sericin, have been the focus for a long time, few researchers have realized the complexity of the silk proteome. We collected sev...
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Published in: | Journal of proteome research 2013-11, Vol.12 (11), p.5213-5222 |
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creator | Dong, Zhaoming Zhao, Ping Wang, Chen Zhang, Yan Chen, Jianping Wang, Xin Lin, Ying Xia, Qingyou |
description | Silkworms (Bombyx mori) produce massive amounts of silk proteins to make cocoons during the final stages of larval development. Although the major components, fibroin and sericin, have been the focus for a long time, few researchers have realized the complexity of the silk proteome. We collected seven kinds of silk fibers spun by silkworm larvae at different developmental stages: the silks spun by new hatched larvae, second instar day 0 larvae, third instar day 0 larvae, fourth instar day 0 larvae, and fourth instar molting larvae, the scaffold silk used to attach the cocoon to the substrate and the cocoon silk. Analysis by liquid chromatography–tandem mass spectrometry identified 500 proteins from the seven silks. In addition to the expected fibroins, sericins, and some known protease inhibitors, we also identified further protease inhibitors, enzymes, proteins of unknown function, and other proteins. Unsurprisingly, our quantitative results showed fibroins and sericins were the most abundant proteins in all seven silks. Except for fibroins and sericins, protease inhibitors, enzymes, and proteins of unknown function were more abundant than other proteins. We found significant change in silk protein compositions through development, being consistent with their different biological functions and complicated formation. |
doi_str_mv | 10.1021/pr4005772 |
format | article |
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Although the major components, fibroin and sericin, have been the focus for a long time, few researchers have realized the complexity of the silk proteome. We collected seven kinds of silk fibers spun by silkworm larvae at different developmental stages: the silks spun by new hatched larvae, second instar day 0 larvae, third instar day 0 larvae, fourth instar day 0 larvae, and fourth instar molting larvae, the scaffold silk used to attach the cocoon to the substrate and the cocoon silk. Analysis by liquid chromatography–tandem mass spectrometry identified 500 proteins from the seven silks. In addition to the expected fibroins, sericins, and some known protease inhibitors, we also identified further protease inhibitors, enzymes, proteins of unknown function, and other proteins. Unsurprisingly, our quantitative results showed fibroins and sericins were the most abundant proteins in all seven silks. Except for fibroins and sericins, protease inhibitors, enzymes, and proteins of unknown function were more abundant than other proteins. We found significant change in silk protein compositions through development, being consistent with their different biological functions and complicated formation.</description><identifier>ISSN: 1535-3893</identifier><identifier>EISSN: 1535-3907</identifier><identifier>DOI: 10.1021/pr4005772</identifier><identifier>PMID: 24093152</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Bombyx - genetics ; Bombyx - growth & development ; Bombyx - metabolism ; Chromatography, Liquid ; Enzymes - metabolism ; Gene Expression Regulation, Developmental - genetics ; Gene Ontology ; Proteomics - methods ; Silk - genetics ; Silk - metabolism ; Tandem Mass Spectrometry</subject><ispartof>Journal of proteome research, 2013-11, Vol.12 (11), p.5213-5222</ispartof><rights>Copyright © 2013 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a315t-4a64144515765900942505c5f72320a9bb1881e76bbbc460a0a0e1f90aa0086a3</citedby><cites>FETCH-LOGICAL-a315t-4a64144515765900942505c5f72320a9bb1881e76bbbc460a0a0e1f90aa0086a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24093152$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dong, Zhaoming</creatorcontrib><creatorcontrib>Zhao, Ping</creatorcontrib><creatorcontrib>Wang, Chen</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Chen, Jianping</creatorcontrib><creatorcontrib>Wang, Xin</creatorcontrib><creatorcontrib>Lin, Ying</creatorcontrib><creatorcontrib>Xia, Qingyou</creatorcontrib><title>Comparative Proteomics Reveal Diverse Functions and Dynamic Changes of Bombyx mori Silk Proteins Spun from Different Development Stages</title><title>Journal of proteome research</title><addtitle>J. Proteome Res</addtitle><description>Silkworms (Bombyx mori) produce massive amounts of silk proteins to make cocoons during the final stages of larval development. Although the major components, fibroin and sericin, have been the focus for a long time, few researchers have realized the complexity of the silk proteome. We collected seven kinds of silk fibers spun by silkworm larvae at different developmental stages: the silks spun by new hatched larvae, second instar day 0 larvae, third instar day 0 larvae, fourth instar day 0 larvae, and fourth instar molting larvae, the scaffold silk used to attach the cocoon to the substrate and the cocoon silk. Analysis by liquid chromatography–tandem mass spectrometry identified 500 proteins from the seven silks. In addition to the expected fibroins, sericins, and some known protease inhibitors, we also identified further protease inhibitors, enzymes, proteins of unknown function, and other proteins. Unsurprisingly, our quantitative results showed fibroins and sericins were the most abundant proteins in all seven silks. Except for fibroins and sericins, protease inhibitors, enzymes, and proteins of unknown function were more abundant than other proteins. We found significant change in silk protein compositions through development, being consistent with their different biological functions and complicated formation.</description><subject>Animals</subject><subject>Bombyx - genetics</subject><subject>Bombyx - growth & development</subject><subject>Bombyx - metabolism</subject><subject>Chromatography, Liquid</subject><subject>Enzymes - metabolism</subject><subject>Gene Expression Regulation, Developmental - genetics</subject><subject>Gene Ontology</subject><subject>Proteomics - methods</subject><subject>Silk - genetics</subject><subject>Silk - metabolism</subject><subject>Tandem Mass Spectrometry</subject><issn>1535-3893</issn><issn>1535-3907</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNptkMtOwzAQRS0E4lFY8APIGyRYFMaOnccSWgpISCAK62iSOpAS28FOKvoF_DauCl0hL2Y0Oj6auYQcM7hgwNll6wSATBK-RfaZjOQwyiDZ_uvTLNojB97PAZhMINole1xAFjHJ98n3yOoWHXb1QtEnZztldV16-qwWChs6DmPnFZ30puxqazxFM6PjpcFA0dE7mjflqa3otdXF8otq62o6rZuPtasOH6Ztb2jlrA6yqlJOmY6Og72xrV710w6D45DsVNh4dfRbB-R1cvMyuhs-PN7ej64ehhj27YYCY8GEkOGQWGYAmeASZCmrhEccMCsKlqZMJXFRFKWIAcNTrMoAESCNMRqQs7W3dfazV77Lde1L1TRolO19HuQp5yLhPKDna7R01nunqrx1tUa3zBnkq9zzTe6BPfnV9oVWsw35F3QATtcAlj6f296ZcOU_oh-0lYl0</recordid><startdate>20131101</startdate><enddate>20131101</enddate><creator>Dong, Zhaoming</creator><creator>Zhao, Ping</creator><creator>Wang, Chen</creator><creator>Zhang, Yan</creator><creator>Chen, Jianping</creator><creator>Wang, Xin</creator><creator>Lin, Ying</creator><creator>Xia, Qingyou</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></search><sort><creationdate>20131101</creationdate><title>Comparative Proteomics Reveal Diverse Functions and Dynamic Changes of Bombyx mori Silk Proteins Spun from Different Development Stages</title><author>Dong, Zhaoming ; Zhao, Ping ; Wang, Chen ; Zhang, Yan ; Chen, Jianping ; Wang, Xin ; Lin, Ying ; Xia, Qingyou</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a315t-4a64144515765900942505c5f72320a9bb1881e76bbbc460a0a0e1f90aa0086a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Bombyx - genetics</topic><topic>Bombyx - growth & development</topic><topic>Bombyx - metabolism</topic><topic>Chromatography, Liquid</topic><topic>Enzymes - metabolism</topic><topic>Gene Expression Regulation, Developmental - genetics</topic><topic>Gene Ontology</topic><topic>Proteomics - methods</topic><topic>Silk - genetics</topic><topic>Silk - metabolism</topic><topic>Tandem Mass Spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dong, Zhaoming</creatorcontrib><creatorcontrib>Zhao, Ping</creatorcontrib><creatorcontrib>Wang, Chen</creatorcontrib><creatorcontrib>Zhang, Yan</creatorcontrib><creatorcontrib>Chen, Jianping</creatorcontrib><creatorcontrib>Wang, Xin</creatorcontrib><creatorcontrib>Lin, Ying</creatorcontrib><creatorcontrib>Xia, Qingyou</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><jtitle>Journal of proteome research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dong, Zhaoming</au><au>Zhao, Ping</au><au>Wang, Chen</au><au>Zhang, Yan</au><au>Chen, Jianping</au><au>Wang, Xin</au><au>Lin, Ying</au><au>Xia, Qingyou</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative Proteomics Reveal Diverse Functions and Dynamic Changes of Bombyx mori Silk Proteins Spun from Different Development Stages</atitle><jtitle>Journal of proteome research</jtitle><addtitle>J. Proteome Res</addtitle><date>2013-11-01</date><risdate>2013</risdate><volume>12</volume><issue>11</issue><spage>5213</spage><epage>5222</epage><pages>5213-5222</pages><issn>1535-3893</issn><eissn>1535-3907</eissn><abstract>Silkworms (Bombyx mori) produce massive amounts of silk proteins to make cocoons during the final stages of larval development. Although the major components, fibroin and sericin, have been the focus for a long time, few researchers have realized the complexity of the silk proteome. We collected seven kinds of silk fibers spun by silkworm larvae at different developmental stages: the silks spun by new hatched larvae, second instar day 0 larvae, third instar day 0 larvae, fourth instar day 0 larvae, and fourth instar molting larvae, the scaffold silk used to attach the cocoon to the substrate and the cocoon silk. Analysis by liquid chromatography–tandem mass spectrometry identified 500 proteins from the seven silks. In addition to the expected fibroins, sericins, and some known protease inhibitors, we also identified further protease inhibitors, enzymes, proteins of unknown function, and other proteins. Unsurprisingly, our quantitative results showed fibroins and sericins were the most abundant proteins in all seven silks. Except for fibroins and sericins, protease inhibitors, enzymes, and proteins of unknown function were more abundant than other proteins. We found significant change in silk protein compositions through development, being consistent with their different biological functions and complicated formation.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>24093152</pmid><doi>10.1021/pr4005772</doi><tpages>10</tpages></addata></record> |
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source | American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list) |
subjects | Animals Bombyx - genetics Bombyx - growth & development Bombyx - metabolism Chromatography, Liquid Enzymes - metabolism Gene Expression Regulation, Developmental - genetics Gene Ontology Proteomics - methods Silk - genetics Silk - metabolism Tandem Mass Spectrometry |
title | Comparative Proteomics Reveal Diverse Functions and Dynamic Changes of Bombyx mori Silk Proteins Spun from Different Development Stages |
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