Thioredoxin is related to life span regulation and oxidative stress response in Caenorhabditis elegans
Thioredoxin, an oxidoreductase, is a multifunction protein. The thioredoxin system is composed of NADPH, thioredoxin reductase and thioredoxin. This enzyme is highly conserved from bacteria to humans. We have characterized TRX‐1, a thioredoxin homolog in C. elegans, which has about 36% identity in a...
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| Veröffentlicht in: | Genes to cells : devoted to molecular & cellular mechanisms 2005-12, Vol.10 (12), p.1203-1210 |
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| creator | Jee, Changhoon Vanoaica, Liviu Lee, Jungsoo Park, Byung Jae Ahnn, Joohong |
| description | Thioredoxin, an oxidoreductase, is a multifunction protein. The thioredoxin system is composed of NADPH, thioredoxin reductase and thioredoxin. This enzyme is highly conserved from bacteria to humans. We have characterized TRX‐1, a thioredoxin homolog in C. elegans, which has about 36% identity in amino acid sequence with human thioredoxin. By gfp reporter system, trx‐1 has been shown to be restrictedly expressed in ASI and ASJ neurons and in intestine. Immunostaining confirmed the intestinal expression. Full‐length cDNA of trx‐1 has been isolated by cDNA library PCR and subsequently cloned and sequenced. We have shown that the encoded protein functions as a reductase in the insulin reducing assay. Moreover, we have isolated a deletion mutant by PCR‐based TMP‐UV mutagenesis method. Mutant animals have reduced life span and are sensitive to oxidative stress. Reintroduction of trx‐1 into mutant worms fully restored the wild‐type phenotype. Our results suggest that trx‐1 has important functions in life span regulation and oxidative stress response in C. elegans. |
| doi_str_mv | 10.1111/j.1365-2443.2005.00913.x |
| format | Article |
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The thioredoxin system is composed of NADPH, thioredoxin reductase and thioredoxin. This enzyme is highly conserved from bacteria to humans. We have characterized TRX‐1, a thioredoxin homolog in C. elegans, which has about 36% identity in amino acid sequence with human thioredoxin. By gfp reporter system, trx‐1 has been shown to be restrictedly expressed in ASI and ASJ neurons and in intestine. Immunostaining confirmed the intestinal expression. Full‐length cDNA of trx‐1 has been isolated by cDNA library PCR and subsequently cloned and sequenced. We have shown that the encoded protein functions as a reductase in the insulin reducing assay. Moreover, we have isolated a deletion mutant by PCR‐based TMP‐UV mutagenesis method. Mutant animals have reduced life span and are sensitive to oxidative stress. Reintroduction of trx‐1 into mutant worms fully restored the wild‐type phenotype. Our results suggest that trx‐1 has important functions in life span regulation and oxidative stress response in C. elegans.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - enzymology</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - physiology</subject><subject>Caenorhabditis elegans Proteins - chemistry</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Humans</subject><subject>Life Expectancy</subject><subject>Molecular Sequence Data</subject><subject>Oxidative Stress - genetics</subject><subject>Oxidative Stress - physiology</subject><subject>Oxidoreductases - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Thioredoxins - chemistry</subject><subject>Thioredoxins - genetics</subject><subject>Thioredoxins - metabolism</subject><issn>1356-9597</issn><issn>1365-2443</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEtPAyEUhYnR2Fr9C4aVuxlhmBeJG9NoNWnipq4JhUtLMx0qzGj772Vso1vZcB_fOTc5CGFKUhrf_SalrCySLM9ZmhFSpIRwytL9GRr_Ls6HuigTXvBqhK5C2BBCWUaKSzSiJctyWpRjZBZr6zxot7cttgF7aGQHGncON9YADjvZxuGqj2PrWixbjSOrY_cZt52HMIjCzrUBcPSYSmidX8ultl30gwZWsg3X6MLIJsDN6Z-g9-enxfQlmb_NXqeP80QxXrFEKUM01yBpqSXh3GgADcuaZJlRHEhtmDJcZ7XMuYpt5LNIs1IblVcVYRN0d_TdeffRQ-jE1gYFTSNbcH0QtMrzsi6LCNZHUHkXggcjdt5upT8ISsSQsdiIIUoxRCmGjMVPxmIfpbenG_1yC_pPeAo1Ag9H4Ms2cPi3sZgtprFg34i4jeU</recordid><startdate>200512</startdate><enddate>200512</enddate><creator>Jee, Changhoon</creator><creator>Vanoaica, Liviu</creator><creator>Lee, Jungsoo</creator><creator>Park, Byung Jae</creator><creator>Ahnn, Joohong</creator><general>Blackwell Science Ltd</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200512</creationdate><title>Thioredoxin is related to life span regulation and oxidative stress response in Caenorhabditis elegans</title><author>Jee, Changhoon ; Vanoaica, Liviu ; Lee, Jungsoo ; Park, Byung Jae ; Ahnn, Joohong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3973-ccf0d9dea16da099fdeedeb8022fc9e08f3cf9d28a49ce08ccf2dea36dfc47703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - enzymology</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans - physiology</topic><topic>Caenorhabditis elegans Proteins - chemistry</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Humans</topic><topic>Life Expectancy</topic><topic>Molecular Sequence Data</topic><topic>Oxidative Stress - genetics</topic><topic>Oxidative Stress - physiology</topic><topic>Oxidoreductases - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Thioredoxins - chemistry</topic><topic>Thioredoxins - genetics</topic><topic>Thioredoxins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jee, Changhoon</creatorcontrib><creatorcontrib>Vanoaica, Liviu</creatorcontrib><creatorcontrib>Lee, Jungsoo</creatorcontrib><creatorcontrib>Park, Byung Jae</creatorcontrib><creatorcontrib>Ahnn, Joohong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jee, Changhoon</au><au>Vanoaica, Liviu</au><au>Lee, Jungsoo</au><au>Park, Byung Jae</au><au>Ahnn, Joohong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thioredoxin is related to life span regulation and oxidative stress response in Caenorhabditis elegans</atitle><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle><addtitle>Genes Cells</addtitle><date>2005-12</date><risdate>2005</risdate><volume>10</volume><issue>12</issue><spage>1203</spage><epage>1210</epage><pages>1203-1210</pages><issn>1356-9597</issn><eissn>1365-2443</eissn><abstract>Thioredoxin, an oxidoreductase, is a multifunction protein. The thioredoxin system is composed of NADPH, thioredoxin reductase and thioredoxin. This enzyme is highly conserved from bacteria to humans. We have characterized TRX‐1, a thioredoxin homolog in C. elegans, which has about 36% identity in amino acid sequence with human thioredoxin. By gfp reporter system, trx‐1 has been shown to be restrictedly expressed in ASI and ASJ neurons and in intestine. Immunostaining confirmed the intestinal expression. Full‐length cDNA of trx‐1 has been isolated by cDNA library PCR and subsequently cloned and sequenced. We have shown that the encoded protein functions as a reductase in the insulin reducing assay. Moreover, we have isolated a deletion mutant by PCR‐based TMP‐UV mutagenesis method. Mutant animals have reduced life span and are sensitive to oxidative stress. Reintroduction of trx‐1 into mutant worms fully restored the wild‐type phenotype. Our results suggest that trx‐1 has important functions in life span regulation and oxidative stress response in C. elegans.</abstract><cop>Malden, USA</cop><pub>Blackwell Science Ltd</pub><pmid>16324156</pmid><doi>10.1111/j.1365-2443.2005.00913.x</doi><tpages>8</tpages></addata></record> |
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| source | MEDLINE; Wiley Free Content; Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals |
| subjects | Amino Acid Sequence Animals Caenorhabditis elegans Caenorhabditis elegans - enzymology Caenorhabditis elegans - genetics Caenorhabditis elegans - physiology Caenorhabditis elegans Proteins - chemistry Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Humans Life Expectancy Molecular Sequence Data Oxidative Stress - genetics Oxidative Stress - physiology Oxidoreductases - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Sequence Alignment Thioredoxins - chemistry Thioredoxins - genetics Thioredoxins - metabolism |
| title | Thioredoxin is related to life span regulation and oxidative stress response in Caenorhabditis elegans |
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