| pubmed-article:16575904 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16575904 | lifeskim:mentions | umls-concept:C0172537 | lld:lifeskim |
| pubmed-article:16575904 | lifeskim:mentions | umls-concept:C0525037 | lld:lifeskim |
| pubmed-article:16575904 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:16575904 | lifeskim:mentions | umls-concept:C0040649 | lld:lifeskim |
| pubmed-article:16575904 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:16575904 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
| pubmed-article:16575904 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:16575904 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16575904 | pubmed:dateCreated | 2006-5-1 | lld:pubmed |
| pubmed-article:16575904 | pubmed:abstractText | Previous studies demonstrate that p16, a cyclin-dependent kinase inhibitor and a tumor suppressor, may inhibit matrix metalloproteinase-2 (MMP-2) expression in human cancer cells to suppress tumor invasion and metastasis. However, the detailed mechanism is still unclear. Our results show that p16 inhibits MMP-2 expression via transcriptional repression. Promoter deletion and mutation analysis indicates that p16 acts through the Sp1 transcription factor-binding site located between -72 and -64 bp region from the transcriptional start site of the human MMP-2 promoter to repress gene expression. DNA affinity precipitation assay (DAPA) and chromatin immuno-precipitation (CHIP) assay demonstrate that Sp1 proteins constitutively bind to this consensus sequence in vitro and in vivo. p16 attenuates Sp1 binding to the MMP-2 promoter to suppress gene transcription and overexpression of Sp1 may counteract p16-induced downregulation of MMP-2. CyclinA/CDK complex may directly phosphorylate Sp1 and enhance its DNA-binding activity. Thus, we investigated the effect of p16 on the interaction between cyclin A and Sp1. Our results indicate that p16 induces downregulation of cyclin A and CDK2, reduces the interaction between cyclin A and Sp1, and attenuates phosphorylation of Sp1. Ectoexpression of cyclin A counteracts p16-mediated inhibition of DNA binding of Sp1 and activates MMP-2 promoter activity and mRNA expression. Collectively, our results suggest that p16 suppresses MMP-2 by blocking Sp1-mediated gene transcription. | lld:pubmed |
| pubmed-article:16575904 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16575904 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16575904 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16575904 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16575904 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16575904 | pubmed:issn | 0021-9541 | lld:pubmed |
| pubmed-article:16575904 | pubmed:author | pubmed-author:ChangHui-Chiu... | lld:pubmed |
| pubmed-article:16575904 | pubmed:author | pubmed-author:HungWen-ChunW... | lld:pubmed |
| pubmed-article:16575904 | pubmed:author | pubmed-author:WangChie-Hong... | lld:pubmed |
| pubmed-article:16575904 | pubmed:copyrightInfo | Copyright 2006 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:16575904 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16575904 | pubmed:volume | 208 | lld:pubmed |
| pubmed-article:16575904 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16575904 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16575904 | pubmed:pagination | 246-52 | lld:pubmed |
| pubmed-article:16575904 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:16575904 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16575904 | pubmed:articleTitle | p16 inhibits matrix metalloproteinase-2 expression via suppression of Sp1-mediated gene transcription. | lld:pubmed |
| pubmed-article:16575904 | pubmed:affiliation | Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung, Taiwan. | lld:pubmed |
| pubmed-article:16575904 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16575904 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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