Responsiveness of selenoproteins to dietary selenium
Selenocysteine-containing enzymes that have been identified in mammals include the glutathione peroxidase family (GPX1, GPX2, GPX3, and GPX4), one or more iodothyronine deiodinases and two thioredoxin reductases. Selenoprotein P, a glycoprotein that contains 10 selenocysteine residues per 43 kDa pol...
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| Veröffentlicht in: | Annual review of nutrition 1999-01, Vol.19 (1), p.1-16 |
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| creator | Allan, C.B Lacourciere, G.M Stadtman, T.C |
| description | Selenocysteine-containing enzymes that have been identified in mammals include the glutathione peroxidase family (GPX1, GPX2, GPX3, and GPX4), one or more iodothyronine deiodinases and two thioredoxin reductases. Selenoprotein P, a glycoprotein that contains 10 selenocysteine residues per 43 kDa polypeptide and selenoprotein W, a 10 kDa muscle protein, are unidentified as to function. Levels of all of these selenocysteine-containing proteins in various tissues are affected to different extents by selenium availability. Increased amounts of selenoproteins observed in response to selenium supplementation were shown in several studies to correlate with increases in the corresponding mRNA levels. In general, selenoprotein levels in brain are less sensitive to dietary selenium fluctuation than the corresponding selenoprotein levels in other tissues. |
| doi_str_mv | 10.1146/annurev.nutr.19.1.1 |
| format | Article |
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Selenoprotein P, a glycoprotein that contains 10 selenocysteine residues per 43 kDa polypeptide and selenoprotein W, a 10 kDa muscle protein, are unidentified as to function. Levels of all of these selenocysteine-containing proteins in various tissues are affected to different extents by selenium availability. Increased amounts of selenoproteins observed in response to selenium supplementation were shown in several studies to correlate with increases in the corresponding mRNA levels. In general, selenoprotein levels in brain are less sensitive to dietary selenium fluctuation than the corresponding selenoprotein levels in other tissues.</description><identifier>ISSN: 0199-9885</identifier><identifier>EISSN: 1545-4312</identifier><identifier>DOI: 10.1146/annurev.nutr.19.1.1</identifier><identifier>PMID: 10448514</identifier><identifier>CODEN: ARNTD8</identifier><language>eng</language><publisher>Palo Alto, CA: Annual Reviews</publisher><subject>animal proteins ; animal tissues ; Animals ; Biological and medical sciences ; catalytic activity ; cysteine ; deiodinases ; Diet ; dietary minerals ; enzymes ; Feeding. Feeding behavior ; Fundamental and applied biological sciences. Psychology ; gene expression ; glutathione peroxidase ; Glutathione Peroxidase - metabolism ; Humans ; Iodide Peroxidase - metabolism ; literature reviews ; neoplasms ; nutrient deficiencies ; nutrient sources ; Proteins - metabolism ; RNA ; Selenium ; Selenium - administration & dosage ; Selenoprotein P ; Selenoprotein W ; Selenoproteins ; skin ; thioredoxin reductase ; Thioredoxin-Disulfide Reductase - metabolism ; trace element deficiencies ; Vertebrates: anatomy and physiology, studies on body, several organs or systems</subject><ispartof>Annual review of nutrition, 1999-01, Vol.19 (1), p.1-16</ispartof><rights>1999 INIST-CNRS</rights><rights>Copyright Annual Reviews, Inc. 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-583ea93ca219d2879935e421cdc58b85fcc4169160d77af77af25cc9b5f6dce73</citedby><cites>FETCH-LOGICAL-c447t-583ea93ca219d2879935e421cdc58b85fcc4169160d77af77af25cc9b5f6dce73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4168,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1935499$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10448514$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Allan, C.B</creatorcontrib><creatorcontrib>Lacourciere, G.M</creatorcontrib><creatorcontrib>Stadtman, T.C</creatorcontrib><title>Responsiveness of selenoproteins to dietary selenium</title><title>Annual review of nutrition</title><addtitle>Annu Rev Nutr</addtitle><description>Selenocysteine-containing enzymes that have been identified in mammals include the glutathione peroxidase family (GPX1, GPX2, GPX3, and GPX4), one or more iodothyronine deiodinases and two thioredoxin reductases. Selenoprotein P, a glycoprotein that contains 10 selenocysteine residues per 43 kDa polypeptide and selenoprotein W, a 10 kDa muscle protein, are unidentified as to function. Levels of all of these selenocysteine-containing proteins in various tissues are affected to different extents by selenium availability. Increased amounts of selenoproteins observed in response to selenium supplementation were shown in several studies to correlate with increases in the corresponding mRNA levels. In general, selenoprotein levels in brain are less sensitive to dietary selenium fluctuation than the corresponding selenoprotein levels in other tissues.</description><subject>animal proteins</subject><subject>animal tissues</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>catalytic activity</subject><subject>cysteine</subject><subject>deiodinases</subject><subject>Diet</subject><subject>dietary minerals</subject><subject>enzymes</subject><subject>Feeding. Feeding behavior</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene expression</subject><subject>glutathione peroxidase</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Humans</subject><subject>Iodide Peroxidase - metabolism</subject><subject>literature reviews</subject><subject>neoplasms</subject><subject>nutrient deficiencies</subject><subject>nutrient sources</subject><subject>Proteins - metabolism</subject><subject>RNA</subject><subject>Selenium</subject><subject>Selenium - administration & dosage</subject><subject>Selenoprotein P</subject><subject>Selenoprotein W</subject><subject>Selenoproteins</subject><subject>skin</subject><subject>thioredoxin reductase</subject><subject>Thioredoxin-Disulfide Reductase - metabolism</subject><subject>trace element deficiencies</subject><subject>Vertebrates: anatomy and physiology, studies on body, several organs or systems</subject><issn>0199-9885</issn><issn>1545-4312</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpd0E1LxDAQBuAgiruu_gJBFxFvrZl8tM1RFr9AENQ9h2w6lUo3WZNW8N-bpQuKh5BDnpnMvIScAs0BRHFtnBsCfuVu6EMOKocc9sgUpJCZ4MD2yZSCUpmqKjkhRzF-UEoV5_yQTIAKUUkQUyJeMG68i-0XOoxx7pt5xA6d3wTfY-vivPfzusXehO_xpR3Wx-SgMV3Ek909I8u727fFQ_b0fP-4uHnKrBBln8mKo1HcGgaqZlWpFJcoGNjaympVycZaAYWCgtZlaZrtYdJatZJNUVss-YxcjX3TMJ8Dxl6v22ix64xDP0RdKFUA5yzBi3_www_Bpdk0owI4o6VKiI_IBh9jwEZvQrtOe2mgepuo3iWqt4lqUBo0pKqzXethtcb6T80YYQKXO2CiNV0TjLNt_HVpaaG2v5-PrDFem_eQyPKVUeCUJQFA-Q-sMYs4</recordid><startdate>19990101</startdate><enddate>19990101</enddate><creator>Allan, C.B</creator><creator>Lacourciere, G.M</creator><creator>Stadtman, T.C</creator><general>Annual Reviews</general><general>Annual Reviews, Inc</general><scope>FBQ</scope><scope>IQODW</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>3V.</scope><scope>7RV</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9-</scope><scope>K9.</scope><scope>KB0</scope><scope>M0K</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>19990101</creationdate><title>Responsiveness of selenoproteins to dietary selenium</title><author>Allan, C.B ; Lacourciere, G.M ; Stadtman, T.C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-583ea93ca219d2879935e421cdc58b85fcc4169160d77af77af25cc9b5f6dce73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>animal proteins</topic><topic>animal tissues</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>catalytic activity</topic><topic>cysteine</topic><topic>deiodinases</topic><topic>Diet</topic><topic>dietary minerals</topic><topic>enzymes</topic><topic>Feeding. Feeding behavior</topic><topic>Fundamental and applied biological sciences. 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Selenoprotein P, a glycoprotein that contains 10 selenocysteine residues per 43 kDa polypeptide and selenoprotein W, a 10 kDa muscle protein, are unidentified as to function. Levels of all of these selenocysteine-containing proteins in various tissues are affected to different extents by selenium availability. Increased amounts of selenoproteins observed in response to selenium supplementation were shown in several studies to correlate with increases in the corresponding mRNA levels. In general, selenoprotein levels in brain are less sensitive to dietary selenium fluctuation than the corresponding selenoprotein levels in other tissues.</abstract><cop>Palo Alto, CA</cop><pub>Annual Reviews</pub><pmid>10448514</pmid><doi>10.1146/annurev.nutr.19.1.1</doi><tpages>16</tpages></addata></record> |
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| source | Annual Reviews Complete A-Z List; MEDLINE |
| subjects | animal proteins animal tissues Animals Biological and medical sciences catalytic activity cysteine deiodinases Diet dietary minerals enzymes Feeding. Feeding behavior Fundamental and applied biological sciences. Psychology gene expression glutathione peroxidase Glutathione Peroxidase - metabolism Humans Iodide Peroxidase - metabolism literature reviews neoplasms nutrient deficiencies nutrient sources Proteins - metabolism RNA Selenium Selenium - administration & dosage Selenoprotein P Selenoprotein W Selenoproteins skin thioredoxin reductase Thioredoxin-Disulfide Reductase - metabolism trace element deficiencies Vertebrates: anatomy and physiology, studies on body, several organs or systems |
| title | Responsiveness of selenoproteins to dietary selenium |
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