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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2010-8-17
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pubmed:abstractText |
Reactive oxygen species, specifically hydrogen peroxide (H(2)O(2)), have a significant role in hormone production in thyroid tissue. Although recent studies have demonstrated that dual oxidases are responsible for the H(2)O(2) synthesis needed in thyroid hormone production, our data suggest a pivotal role for superoxide dismutase 3 (SOD3) as a major H(2)O(2)-producing enzyme. According to our results, Sod3 is highly expressed in normal thyroid, and becomes even more abundant in rat goiter models. We showed TSH-stimulated expression of Sod3 via phospholipase C-Ca(2+) and cAMP-protein kinase A, a pathway that might be disrupted in thyroid cancer. In line with this finding, we demonstrated an oncogene-dependent decrease in Sod3 mRNA expression synthesis in thyroid cancer cell models that corresponded to a similar decrease in clinical patient samples, suggesting that SOD3 could be used as a differentiation marker in thyroid cancer. Finally, the functional analysis in thyroid models indicated a moderate role for SOD3 in regulating normal thyroid cell proliferation being in line with our previous observations.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/SOD3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sod3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1479-6821
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pubmed:author |
pubmed-author:BasoloFulvioF,
pubmed-author:CantisaniMaria CMC,
pubmed-author:CastelloneMaria DMD,
pubmed-author:DumontJacques EJE,
pubmed-author:HebrantAlineA,
pubmed-author:HosteCandiceC,
pubmed-author:LaatikainenLilja ELE,
pubmed-author:LaukkanenMikko OMO,
pubmed-author:LaurilaJuha PJP,
pubmed-author:NäsmanJohnnyJ,
pubmed-author:SalernoPaoloP,
pubmed-author:SalvatoreGiulianaG,
pubmed-author:SantoroMassimoM
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pubmed:issnType |
Electronic
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
785-96
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pubmed:meshHeading |
pubmed-meshheading:20576801-Animals,
pubmed-meshheading:20576801-Antigens, Differentiation,
pubmed-meshheading:20576801-Blotting, Western,
pubmed-meshheading:20576801-Calcium,
pubmed-meshheading:20576801-Cell Differentiation,
pubmed-meshheading:20576801-Cell Proliferation,
pubmed-meshheading:20576801-Down-Regulation,
pubmed-meshheading:20576801-Humans,
pubmed-meshheading:20576801-Hydrogen Peroxide,
pubmed-meshheading:20576801-Male,
pubmed-meshheading:20576801-RNA, Messenger,
pubmed-meshheading:20576801-RNA, Small Interfering,
pubmed-meshheading:20576801-Rats,
pubmed-meshheading:20576801-Rats, Sprague-Dawley,
pubmed-meshheading:20576801-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:20576801-Superoxide Dismutase,
pubmed-meshheading:20576801-Superoxides,
pubmed-meshheading:20576801-Thyroid Gland,
pubmed-meshheading:20576801-Thyroid Neoplasms,
pubmed-meshheading:20576801-Tumor Cells, Cultured
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pubmed:year |
2010
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pubmed:articleTitle |
Extracellular superoxide dismutase is a thyroid differentiation marker down-regulated in cancer.
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pubmed:affiliation |
Cellular Therapy Group, Medicity Research Laboratory, University of Turku, Tykistökatu 6A, Turku, Finland.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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