Abstract:
:The cartilage matrix is composed of characteristic components including type II collagen, aggrecan and link protein. In this paper, we report two DNA elements that regulate the link protein gene. Using transient transfection assays with link protein gene constructs in chondrocytes, chloramphenicol acetyl transferase (CAT) assays were used to measure the transcriptional activity of the link protein gene. Previously, we identified an enhancer-like activity within the first intron of the gene. In this paper, we report an active 34 bp (+1390 to +1424) fragment within this region that contains a glucocorticoid-like response element (GRE). Both deletion of, and site-specific mutations within this sequence motif reduced the dexamethasone-inducible activity. The GRE-like sequence from the rat link protein gene, or the homologous sequence from the human link protein gene were included in vectors containing the thymidine kinase promoter linked to the CAT gene (tkCAT). Both human and rat elements transferred the ability to respond to dexamethasone and hydrocortisone with a > 10-fold induction. Deletions through the promoter from -923 to -900 identified a second site required for both glucocorticoid and serum responsiveness. A four base substitution at this site resulted in a loss of serum responsiveness. This region contains an AT-rich element, similar to the AT-rich elements involved in homeotic protein regulation of the growth hormone gene and the muscle creatine kinase gene. Southwestern analysis using oligonucleotides containing the AT-rich element from the link protein gene or the muscle creatine kinase gene, identified a 32 kDa protein band from nuclear extracts of chick chondrocytes. Using these AT-rich oligonucleotides in band-shift analyses, nuclear extracts of chick sternal muscle, rat chondrosarcoma and chick sternal chondrocytes each showed formation of different complexes suggesting cell specificity. AT-rich elements have been identified as binding sites for homeodomain-containing proteins and can contribute to gene regulation by serum response factors. The identification of an AT-rich element in the link protein gene suggests similar functions for this element.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Rhodes C,Yamada Ydoi
10.1093/nar/23.12.2305subject
Has Abstractpub_date
1995-06-25 00:00:00pages
2305-13issue
12eissn
0305-1048issn
1362-4962pii
5g0001journal_volume
23pub_type
杂志文章abstract::It is a central issue to elucidate the new type of molecular recognition accompanied by a global structural change of a molecule upon binding to its targets. Here we investigate the driving force for the binding of R12 (a ribonucleic acid aptamer) and P16 (a partial peptide of a prion protein) during which P16 exhibit...
journal_title:Nucleic acids research
pub_type: 杂志文章
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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更新日期:1994-10-11 00:00:00
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更新日期:1997-03-01 00:00:00
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journal_title:Nucleic acids research
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更新日期:1984-09-25 00:00:00
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journal_title:Nucleic acids research
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更新日期:2008-01-01 00:00:00
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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更新日期:2005-06-16 00:00:00
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journal_title:Nucleic acids research
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更新日期:1998-04-15 00:00:00
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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更新日期:1998-12-15 00:00:00
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
pub_type: 杂志文章
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更新日期:1998-02-15 00:00:00
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journal_title:Nucleic acids research
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更新日期:2014-05-01 00:00:00
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更新日期:2000-11-15 00:00:00
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journal_title:Nucleic acids research
pub_type: 杂志文章
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更新日期:1984-02-10 00:00:00