Loading…

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...

Full description

Saved in:
Bibliographic Details
Published in:Journal of proteome research 2013-11, Vol.12 (11), p.5213-5222
Main Authors: Dong, Zhaoming, Zhao, Ping, Wang, Chen, Zhang, Yan, Chen, Jianping, Wang, Xin, Lin, Ying, Xia, Qingyou
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-a315t-4a64144515765900942505c5f72320a9bb1881e76bbbc460a0a0e1f90aa0086a3
cites cdi_FETCH-LOGICAL-a315t-4a64144515765900942505c5f72320a9bb1881e76bbbc460a0a0e1f90aa0086a3
container_end_page 5222
container_issue 11
container_start_page 5213
container_title Journal of proteome research
container_volume 12
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
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1448224722</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1448224722</sourcerecordid><originalsourceid>FETCH-LOGICAL-a315t-4a64144515765900942505c5f72320a9bb1881e76bbbc460a0a0e1f90aa0086a3</originalsourceid><addsrcrecordid>eNptkMtOwzAQRS0E4lFY8APIGyRYFMaOnccSWgpISCAK62iSOpAS28FOKvoF_DauCl0hL2Y0Oj6auYQcM7hgwNll6wSATBK-RfaZjOQwyiDZ_uvTLNojB97PAZhMINole1xAFjHJ98n3yOoWHXb1QtEnZztldV16-qwWChs6DmPnFZ30puxqazxFM6PjpcFA0dE7mjflqa3otdXF8otq62o6rZuPtasOH6Ztb2jlrA6yqlJOmY6Og72xrV710w6D45DsVNh4dfRbB-R1cvMyuhs-PN7ej64ehhj27YYCY8GEkOGQWGYAmeASZCmrhEccMCsKlqZMJXFRFKWIAcNTrMoAESCNMRqQs7W3dfazV77Lde1L1TRolO19HuQp5yLhPKDna7R01nunqrx1tUa3zBnkq9zzTe6BPfnV9oVWsw35F3QATtcAlj6f296ZcOU_oh-0lYl0</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1448224722</pqid></control><display><type>article</type><title>Comparative Proteomics Reveal Diverse Functions and Dynamic Changes of Bombyx mori Silk Proteins Spun from Different Development Stages</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read &amp; Publish Agreement 2022-2024 (Reading list)</source><creator>Dong, Zhaoming ; Zhao, Ping ; Wang, Chen ; Zhang, Yan ; Chen, Jianping ; Wang, Xin ; Lin, Ying ; Xia, Qingyou</creator><creatorcontrib>Dong, Zhaoming ; Zhao, Ping ; Wang, Chen ; Zhang, Yan ; Chen, Jianping ; Wang, Xin ; Lin, Ying ; Xia, Qingyou</creatorcontrib><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><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 &amp; 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 &amp; 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 &amp; 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>
fulltext fulltext
identifier ISSN: 1535-3893
ispartof Journal of proteome research, 2013-11, Vol.12 (11), p.5213-5222
issn 1535-3893
1535-3907
language eng
recordid cdi_proquest_miscellaneous_1448224722
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
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T01%3A59%3A43IST&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=Comparative%20Proteomics%20Reveal%20Diverse%20Functions%20and%20Dynamic%20Changes%20of%20Bombyx%20mori%20Silk%20Proteins%20Spun%20from%20Different%20Development%20Stages&rft.jtitle=Journal%20of%20proteome%20research&rft.au=Dong,%20Zhaoming&rft.date=2013-11-01&rft.volume=12&rft.issue=11&rft.spage=5213&rft.epage=5222&rft.pages=5213-5222&rft.issn=1535-3893&rft.eissn=1535-3907&rft_id=info:doi/10.1021/pr4005772&rft_dat=%3Cproquest_cross%3E1448224722%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a315t-4a64144515765900942505c5f72320a9bb1881e76bbbc460a0a0e1f90aa0086a3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1448224722&rft_id=info:pmid/24093152&rfr_iscdi=true