Duox1 is the main source of hydrogen peroxide in the rat thyroid cell line PCCl3
Duox1 and Duox2 proteins are particular members of the NADPH oxidase (Nox) family and were first characterized as the thyroid NADPH oxidases. These proteins are responsible for the hydrogen peroxide (H 2O 2) production necessary for the synthesis of thyroid hormones. Although mutations in the Duox2...
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| Veröffentlicht in: | Experimental cell research 2007-11, Vol.313 (18), p.3892-3901 |
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| creator | Rigutto, Sabrina Hoste, Candice Dumont, Jacques E. Corvilain, Bernard Miot, Françoise De Deken, Xavier |
| description | Duox1 and Duox2 proteins are particular members of the NADPH oxidase (Nox) family and were first characterized as the thyroid NADPH oxidases. These proteins are responsible for the hydrogen peroxide (H
2O
2) production necessary for the synthesis of thyroid hormones. Although mutations in the
Duox2 gene have been discovered in hypothyroid patients with iodide organification defects, attempts to confirm the role of one or both proteins in the generation of H
2O
2 in the thyroid were unfruitful. Using the RNA interference technique, we demonstrated in this study that Duox1 is the main source of H
2O
2 in the rat thyroid cell line PCCl3. We showed that (1) Duox1 was abundantly expressed in PCCl3 in regard to Duox2, contrary to what was observed in the rat thyroid tissue; (2) the expression of a siRNA specifically targeting Duox1-induced silencing of its transcript and the corresponding protein with a parallel decrease of H
2O
2 production; (3) the re-expression of Duox1 in silenced cells by a lentivirus based method rescued totally H
2O
2 production with rat Duox1 and partially with human Duox1. Western blotting analysis confirmed the synthesis of the mature N-linked glycosylated protein responsible for this enzymatic activity. |
| doi_str_mv | 10.1016/j.yexcr.2007.06.011 |
| format | Article |
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2O
2) production necessary for the synthesis of thyroid hormones. Although mutations in the
Duox2 gene have been discovered in hypothyroid patients with iodide organification defects, attempts to confirm the role of one or both proteins in the generation of H
2O
2 in the thyroid were unfruitful. Using the RNA interference technique, we demonstrated in this study that Duox1 is the main source of H
2O
2 in the rat thyroid cell line PCCl3. We showed that (1) Duox1 was abundantly expressed in PCCl3 in regard to Duox2, contrary to what was observed in the rat thyroid tissue; (2) the expression of a siRNA specifically targeting Duox1-induced silencing of its transcript and the corresponding protein with a parallel decrease of H
2O
2 production; (3) the re-expression of Duox1 in silenced cells by a lentivirus based method rescued totally H
2O
2 production with rat Duox1 and partially with human Duox1. Western blotting analysis confirmed the synthesis of the mature N-linked glycosylated protein responsible for this enzymatic activity.</description><identifier>ISSN: 0014-4827</identifier><identifier>EISSN: 1090-2422</identifier><identifier>DOI: 10.1016/j.yexcr.2007.06.011</identifier><identifier>PMID: 17643428</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell Line ; Cellular biology ; CHO Cells ; Clone Cells ; Cricetinae ; Cricetulus ; Dual Oxidases ; Duox ; Enzymes ; Flavoproteins - genetics ; Flavoproteins - metabolism ; Gene Expression ; Gene Expression Regulation ; Gene Silencing ; H 2O 2 ; Humans ; Hydrogen Peroxide - metabolism ; Iodides - metabolism ; Lentivirus ; NADPH oxidase ; NADPH Oxidases ; NOX ; PCCl3 ; Rats ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA, Small Interfering - metabolism ; Rodents ; siRNA ; Thyroid ; Thyroid gland ; Thyroid Gland - cytology ; Thyroid Gland - metabolism</subject><ispartof>Experimental cell research, 2007-11, Vol.313 (18), p.3892-3901</ispartof><rights>2007 Elsevier Inc.</rights><rights>Copyright © 2007 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c299t-43861610bd8d3fe60cf2b0637971d6145b63cf4b62473e9ba674af7432165fbd3</citedby><cites>FETCH-LOGICAL-c299t-43861610bd8d3fe60cf2b0637971d6145b63cf4b62473e9ba674af7432165fbd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014482707002893$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17643428$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rigutto, Sabrina</creatorcontrib><creatorcontrib>Hoste, Candice</creatorcontrib><creatorcontrib>Dumont, Jacques E.</creatorcontrib><creatorcontrib>Corvilain, Bernard</creatorcontrib><creatorcontrib>Miot, Françoise</creatorcontrib><creatorcontrib>De Deken, Xavier</creatorcontrib><title>Duox1 is the main source of hydrogen peroxide in the rat thyroid cell line PCCl3</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>Duox1 and Duox2 proteins are particular members of the NADPH oxidase (Nox) family and were first characterized as the thyroid NADPH oxidases. These proteins are responsible for the hydrogen peroxide (H
2O
2) production necessary for the synthesis of thyroid hormones. Although mutations in the
Duox2 gene have been discovered in hypothyroid patients with iodide organification defects, attempts to confirm the role of one or both proteins in the generation of H
2O
2 in the thyroid were unfruitful. Using the RNA interference technique, we demonstrated in this study that Duox1 is the main source of H
2O
2 in the rat thyroid cell line PCCl3. We showed that (1) Duox1 was abundantly expressed in PCCl3 in regard to Duox2, contrary to what was observed in the rat thyroid tissue; (2) the expression of a siRNA specifically targeting Duox1-induced silencing of its transcript and the corresponding protein with a parallel decrease of H
2O
2 production; (3) the re-expression of Duox1 in silenced cells by a lentivirus based method rescued totally H
2O
2 production with rat Duox1 and partially with human Duox1. Western blotting analysis confirmed the synthesis of the mature N-linked glycosylated protein responsible for this enzymatic activity.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Cellular biology</subject><subject>CHO Cells</subject><subject>Clone Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>Dual Oxidases</subject><subject>Duox</subject><subject>Enzymes</subject><subject>Flavoproteins - genetics</subject><subject>Flavoproteins - metabolism</subject><subject>Gene Expression</subject><subject>Gene Expression Regulation</subject><subject>Gene Silencing</subject><subject>H 2O 2</subject><subject>Humans</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Iodides - metabolism</subject><subject>Lentivirus</subject><subject>NADPH oxidase</subject><subject>NADPH Oxidases</subject><subject>NOX</subject><subject>PCCl3</subject><subject>Rats</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Rodents</subject><subject>siRNA</subject><subject>Thyroid</subject><subject>Thyroid gland</subject><subject>Thyroid Gland - cytology</subject><subject>Thyroid Gland - metabolism</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi1ERZfCL0BCFgduSWds104OHNDyVakSPcDZSuwJ9SobL3ZS7f77etmVkDhwmsM873w8jL1BqBFQX2_qA-1dqgWAqUHXgPiMrRBaqIQS4jlbAaCqVCPMJXuZ8wYAmgb1C3aJRiupRLNi95-WuEceMp8fiG-7MPEcl-SIx4E_HHyKv2jiO0pxHzzx0j5yqZtLPaQYPHc0jnwME_H79XqUr9jF0I2ZXp_rFfv55fOP9bfq7vvX2_XHu8qJtp0rJRuNGqH3jZcDaXCD6EFL0xr0GtVNr6UbVK-FMpLavtNGdYNRUqC-GXovr9j709xdir8XyrPdhny8pZsoLtnqRqGUEgv47h9wUx6cym0WW6VNCwgFkifIpZhzosHuUth26WAR7NG23dg_tu3RtgVti-2SensevfRb8n8zZ70F-HACqJh4DJRsdoEmRz4kcrP1Mfx3wRMQg49E</recordid><startdate>20071101</startdate><enddate>20071101</enddate><creator>Rigutto, Sabrina</creator><creator>Hoste, Candice</creator><creator>Dumont, Jacques E.</creator><creator>Corvilain, Bernard</creator><creator>Miot, Françoise</creator><creator>De Deken, Xavier</creator><general>Elsevier Inc</general><general>Elsevier BV</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>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20071101</creationdate><title>Duox1 is the main source of hydrogen peroxide in the rat thyroid cell line PCCl3</title><author>Rigutto, Sabrina ; Hoste, Candice ; Dumont, Jacques E. ; Corvilain, Bernard ; Miot, Françoise ; De Deken, Xavier</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c299t-43861610bd8d3fe60cf2b0637971d6145b63cf4b62473e9ba674af7432165fbd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Cellular biology</topic><topic>CHO Cells</topic><topic>Clone Cells</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>Dual Oxidases</topic><topic>Duox</topic><topic>Enzymes</topic><topic>Flavoproteins - genetics</topic><topic>Flavoproteins - metabolism</topic><topic>Gene Expression</topic><topic>Gene Expression Regulation</topic><topic>Gene Silencing</topic><topic>H 2O 2</topic><topic>Humans</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Iodides - metabolism</topic><topic>Lentivirus</topic><topic>NADPH oxidase</topic><topic>NADPH Oxidases</topic><topic>NOX</topic><topic>PCCl3</topic><topic>Rats</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA, Small Interfering - metabolism</topic><topic>Rodents</topic><topic>siRNA</topic><topic>Thyroid</topic><topic>Thyroid gland</topic><topic>Thyroid Gland - cytology</topic><topic>Thyroid Gland - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rigutto, Sabrina</creatorcontrib><creatorcontrib>Hoste, Candice</creatorcontrib><creatorcontrib>Dumont, Jacques E.</creatorcontrib><creatorcontrib>Corvilain, Bernard</creatorcontrib><creatorcontrib>Miot, Françoise</creatorcontrib><creatorcontrib>De Deken, Xavier</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rigutto, Sabrina</au><au>Hoste, Candice</au><au>Dumont, Jacques E.</au><au>Corvilain, Bernard</au><au>Miot, Françoise</au><au>De Deken, Xavier</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Duox1 is the main source of hydrogen peroxide in the rat thyroid cell line PCCl3</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>2007-11-01</date><risdate>2007</risdate><volume>313</volume><issue>18</issue><spage>3892</spage><epage>3901</epage><pages>3892-3901</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><abstract>Duox1 and Duox2 proteins are particular members of the NADPH oxidase (Nox) family and were first characterized as the thyroid NADPH oxidases. These proteins are responsible for the hydrogen peroxide (H
2O
2) production necessary for the synthesis of thyroid hormones. Although mutations in the
Duox2 gene have been discovered in hypothyroid patients with iodide organification defects, attempts to confirm the role of one or both proteins in the generation of H
2O
2 in the thyroid were unfruitful. Using the RNA interference technique, we demonstrated in this study that Duox1 is the main source of H
2O
2 in the rat thyroid cell line PCCl3. We showed that (1) Duox1 was abundantly expressed in PCCl3 in regard to Duox2, contrary to what was observed in the rat thyroid tissue; (2) the expression of a siRNA specifically targeting Duox1-induced silencing of its transcript and the corresponding protein with a parallel decrease of H
2O
2 production; (3) the re-expression of Duox1 in silenced cells by a lentivirus based method rescued totally H
2O
2 production with rat Duox1 and partially with human Duox1. Western blotting analysis confirmed the synthesis of the mature N-linked glycosylated protein responsible for this enzymatic activity.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17643428</pmid><doi>10.1016/j.yexcr.2007.06.011</doi><tpages>10</tpages></addata></record> |
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| ispartof | Experimental cell research, 2007-11, Vol.313 (18), p.3892-3901 |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Cell Line Cellular biology CHO Cells Clone Cells Cricetinae Cricetulus Dual Oxidases Duox Enzymes Flavoproteins - genetics Flavoproteins - metabolism Gene Expression Gene Expression Regulation Gene Silencing H 2O 2 Humans Hydrogen Peroxide - metabolism Iodides - metabolism Lentivirus NADPH oxidase NADPH Oxidases NOX PCCl3 Rats RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Small Interfering - metabolism Rodents siRNA Thyroid Thyroid gland Thyroid Gland - cytology Thyroid Gland - metabolism |
| title | Duox1 is the main source of hydrogen peroxide in the rat thyroid cell line PCCl3 |
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