Mass spectrometric proteome analysis for profiling temperature-dependent changes of protein expression in wild-type Caenorhabditis elegans
We investigated the effect of cultivation temperatures on the protein expression levels in the fourth larval stage of the postembryonic development of wild‐type Caenorhabditis elegans by mass spectrometric proteome analysis. From the 64 protein spots that were investigated, 5 spots were found reprod...
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Veröffentlicht in: | Proteomics (Weinheim) 2003-08, Vol.3 (8), p.1526-1534 |
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creator | Mádi, András Mikkat, Stefan Ringel, Bruno Ulbrich, Markus Thiesen, Hans-Jürgen Glocker, Michael O. |
description | We investigated the effect of cultivation temperatures on the protein expression levels in the fourth larval stage of the postembryonic development of wild‐type Caenorhabditis elegans by mass spectrometric proteome analysis. From the 64 protein spots that were investigated, 5 spots were found reproducibly differently expressed when proteome maps derived from animals kept at 15°C and at 25°C, respectively, were compared. Spots of heat shock proteins HSP 70 (CE18679 or CE09682) and HSP 16 (CE14249) were present only in gels from protein extracts when worms were grown at 15°C. Spots of two metabolic enzymes, the isocitrate dehydrogenase (CE10345) and the aspartic proteinase (CE21681) were detected only in cultures grown at the lower temperature as well. A protein with still unknown function (CE05036) was present only in gels from worm samples grown at 25°C. We show for the first time by proteome analyses that cultivation of worms at the lowest temperature of the known physiological range (15°C) already triggers a (weak) stress response in wild‐type animals. This work led to the identification of “internal control proteins” in the wild‐type strain for further characterization of temperature‐sensitive strains using a proteomics approach. |
doi_str_mv | 10.1002/pmic.200300490 |
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From the 64 protein spots that were investigated, 5 spots were found reproducibly differently expressed when proteome maps derived from animals kept at 15°C and at 25°C, respectively, were compared. Spots of heat shock proteins HSP 70 (CE18679 or CE09682) and HSP 16 (CE14249) were present only in gels from protein extracts when worms were grown at 15°C. Spots of two metabolic enzymes, the isocitrate dehydrogenase (CE10345) and the aspartic proteinase (CE21681) were detected only in cultures grown at the lower temperature as well. A protein with still unknown function (CE05036) was present only in gels from worm samples grown at 25°C. We show for the first time by proteome analyses that cultivation of worms at the lowest temperature of the known physiological range (15°C) already triggers a (weak) stress response in wild‐type animals. This work led to the identification of “internal control proteins” in the wild‐type strain for further characterization of temperature‐sensitive strains using a proteomics approach.</description><identifier>ISSN: 1615-9853</identifier><identifier>EISSN: 1615-9861</identifier><identifier>DOI: 10.1002/pmic.200300490</identifier><identifier>PMID: 12923778</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Amino Acid Sequence ; Animals ; Caenorhabditis elegans ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - metabolism ; Electrophoresis, Gel, Two-Dimensional ; Fourth larval stage ; Mass Spectrometry - methods ; Matrix assisted laser desorption/ionization-time of flight-mass spectrometry ; Molecular Sequence Data ; Proteome ; Sequence Homology, Amino Acid ; Temperature ; Temperature-sensitive strains</subject><ispartof>Proteomics (Weinheim), 2003-08, Vol.3 (8), p.1526-1534</ispartof><rights>Copyright © 2003 WILEY‐VCH Verlag GmbH & Co. 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From the 64 protein spots that were investigated, 5 spots were found reproducibly differently expressed when proteome maps derived from animals kept at 15°C and at 25°C, respectively, were compared. Spots of heat shock proteins HSP 70 (CE18679 or CE09682) and HSP 16 (CE14249) were present only in gels from protein extracts when worms were grown at 15°C. Spots of two metabolic enzymes, the isocitrate dehydrogenase (CE10345) and the aspartic proteinase (CE21681) were detected only in cultures grown at the lower temperature as well. A protein with still unknown function (CE05036) was present only in gels from worm samples grown at 25°C. We show for the first time by proteome analyses that cultivation of worms at the lowest temperature of the known physiological range (15°C) already triggers a (weak) stress response in wild‐type animals. This work led to the identification of “internal control proteins” in the wild‐type strain for further characterization of temperature‐sensitive strains using a proteomics approach.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Fourth larval stage</subject><subject>Mass Spectrometry - methods</subject><subject>Matrix assisted laser desorption/ionization-time of flight-mass spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Proteome</subject><subject>Sequence Homology, Amino Acid</subject><subject>Temperature</subject><subject>Temperature-sensitive strains</subject><issn>1615-9853</issn><issn>1615-9861</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1u1DAUhS1ERX9gyxJ5xS6DnR87XqIApVKnrRAIdtaNfTM1JE5qe0TnFXjqZpTRwI6Vfe3vfLo6hLzmbMUZy99NgzOrnLGCsVKxZ-SMC15lqhb8-fFeFafkPMafjHFZK_mCnPJc5YWU9Rn5s4YYaZzQpDAOmIIzdApjwnmg4KHfRRdpN4b9a-d65zc04TBhgLQNmFmc0Fv0iZp78BuMdOwWgfMUH6eAMbrR03n67Xqbpd2EtAH0Y7iH1ro027HHDfj4kpx00Ed8dTgvyLdPH782n7Pr28ur5v11ZgqpWCaN5QqEYajqtkRjTQVMYJcDa6EtW1ODgk5UyCwoW9qyq_j8r7gqESoGxQV5u3jnNR-2GJMeXDTY9-Bx3EYti0qIXPAZXC2gCWOMATs9BTdA2GnO9L59vW9fH9ufA28O5m07oP2LH-qeAbUAcxe4-49O362vmn_l2ZJ1MeHjMQvhlxaykJX-fnOpBfuw_lI2tf5RPAFPOaYT</recordid><startdate>200308</startdate><enddate>200308</enddate><creator>Mádi, András</creator><creator>Mikkat, Stefan</creator><creator>Ringel, Bruno</creator><creator>Ulbrich, Markus</creator><creator>Thiesen, Hans-Jürgen</creator><creator>Glocker, Michael O.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>200308</creationdate><title>Mass spectrometric proteome analysis for profiling temperature-dependent changes of protein expression in wild-type Caenorhabditis elegans</title><author>Mádi, András ; Mikkat, Stefan ; Ringel, Bruno ; Ulbrich, Markus ; Thiesen, Hans-Jürgen ; Glocker, Michael O.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3790-7cd19a6c0e98b4ecdc5a06ef2a0bab4bc8a9af65e0da9d4d4f5106e9194ea50a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Fourth larval stage</topic><topic>Mass Spectrometry - methods</topic><topic>Matrix assisted laser desorption/ionization-time of flight-mass spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Proteome</topic><topic>Sequence Homology, Amino Acid</topic><topic>Temperature</topic><topic>Temperature-sensitive strains</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mádi, András</creatorcontrib><creatorcontrib>Mikkat, Stefan</creatorcontrib><creatorcontrib>Ringel, Bruno</creatorcontrib><creatorcontrib>Ulbrich, Markus</creatorcontrib><creatorcontrib>Thiesen, Hans-Jürgen</creatorcontrib><creatorcontrib>Glocker, Michael O.</creatorcontrib><collection>Istex</collection><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>Proteomics (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mádi, András</au><au>Mikkat, Stefan</au><au>Ringel, Bruno</au><au>Ulbrich, Markus</au><au>Thiesen, Hans-Jürgen</au><au>Glocker, Michael O.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mass spectrometric proteome analysis for profiling temperature-dependent changes of protein expression in wild-type Caenorhabditis elegans</atitle><jtitle>Proteomics (Weinheim)</jtitle><addtitle>Proteomics</addtitle><date>2003-08</date><risdate>2003</risdate><volume>3</volume><issue>8</issue><spage>1526</spage><epage>1534</epage><pages>1526-1534</pages><issn>1615-9853</issn><eissn>1615-9861</eissn><abstract>We investigated the effect of cultivation temperatures on the protein expression levels in the fourth larval stage of the postembryonic development of wild‐type Caenorhabditis elegans by mass spectrometric proteome analysis. From the 64 protein spots that were investigated, 5 spots were found reproducibly differently expressed when proteome maps derived from animals kept at 15°C and at 25°C, respectively, were compared. Spots of heat shock proteins HSP 70 (CE18679 or CE09682) and HSP 16 (CE14249) were present only in gels from protein extracts when worms were grown at 15°C. Spots of two metabolic enzymes, the isocitrate dehydrogenase (CE10345) and the aspartic proteinase (CE21681) were detected only in cultures grown at the lower temperature as well. A protein with still unknown function (CE05036) was present only in gels from worm samples grown at 25°C. We show for the first time by proteome analyses that cultivation of worms at the lowest temperature of the known physiological range (15°C) already triggers a (weak) stress response in wild‐type animals. This work led to the identification of “internal control proteins” in the wild‐type strain for further characterization of temperature‐sensitive strains using a proteomics approach.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>12923778</pmid><doi>10.1002/pmic.200300490</doi><tpages>9</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Caenorhabditis elegans Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - metabolism Electrophoresis, Gel, Two-Dimensional Fourth larval stage Mass Spectrometry - methods Matrix assisted laser desorption/ionization-time of flight-mass spectrometry Molecular Sequence Data Proteome Sequence Homology, Amino Acid Temperature Temperature-sensitive strains |
title | Mass spectrometric proteome analysis for profiling temperature-dependent changes of protein expression in wild-type Caenorhabditis elegans |
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