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http://purl.uniprot.org/citations/11278550http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11278550http://www.w3.org/2000/01/rdf-schema#comment"Manganese superoxide dismutase (Mn-SOD) is a primary antioxidant enzyme whose expression is essential for life in oxygen. Mn-SOD has tumor suppressor activity in a wide variety of tumors and transformed cell systems. Our initial observations revealed that Mn-SOD expression was inversely correlated with expression of AP-2 transcription factors in normal human fibroblasts and their SV-40 transformed counterparts. Thus we hypothesized that AP-2 may down-regulate Mn-SOD expression. To examine the functional role of AP-2 on Mn-SOD promoter transactivation we cotransfected AP-2-deficient HepG2 cells with a human Mn-SOD promoter-reporter construct and expression vectors encoding each of the three known AP-2 family members. Our results indicated that AP-2 could significantly repress Mn-SOD promoter activity, and that this repression was both Mn-SOD promoter and AP-2-specific. The three AP-2 proteins appeared to play distinct roles in Mn-SOD gene regulation. Moreover, although all three AP-2 proteins could repress the Mn-SOD promoter, AP-2alpha and AP-2gamma were more active in this regard than AP-2beta. Transcriptional repression by AP-2 was not a general effect in this system, because another AP-2-responsive gene, c-erbB-3, was transactivated by AP-2. Repression of Mn-SOD by AP-2 was dependent on DNA binding, and expression of AP-2B, a dominant negative incapable of DNA binding, relieved the repression on Mn-SOD promoter and reactivated Mn-SOD expression in the AP-2 abundant SV40-transformed fibroblast cell line MRC-5VA. These results indicate that AP-2-mediated transcriptional repression contributes to the constitutively low expression of Mn-SOD in SV40-transformed fibroblasts and suggest a mechanism for Mn-SOD down-regulation in cancer."xsd:string
http://purl.uniprot.org/citations/11278550http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m009708200"xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/author"Huang Y."xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/author"Zhu C.H."xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/author"Domann F.E."xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/author"Oberley L.W."xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/pages"14407-14413"xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/title"A family of AP-2 proteins down-regulate manganese superoxide dismutase expression."xsd:string
http://purl.uniprot.org/citations/11278550http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11278550http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11278550
http://purl.uniprot.org/citations/11278550http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11278550
http://purl.uniprot.org/uniprot/Q92754#attribution-BA94CB2AAF030235EEAD0087F9781F8Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/11278550
http://purl.uniprot.org/uniprot/P05549#attribution-BA94CB2AAF030235EEAD0087F9781F8Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/11278550