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Characterization of 5′-flanking region of human aggrecanase-1 (ADAMTS4) gene (2000)

Mizui, Yoshiharu ; Yamazaki, Kazuto ; Kuboi, Yoshikazu ; [et al.]

Springer

Molecular biology reports 27 (2000), S. 167-173

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ISSN: 1573-4978

Keywords: aggrecanase-1 ; ADAMTS4 ; promoter ; silencer ; nuclear factor I

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Aggrecanase-1, also known as ADAMTS4 (a disintegrin and metalloproteinase with thrombospondin motifs 4), cleaves at the Glu373-Ala374 site of aggrecan, thereby indicating aggrecan degradation. It is thought that ADAMTS4 plays a pivotal role in inflammatory joint diseases and cartilage degradation. To elucidate the mechanisms of regulation of ADAMTS4 gene expression, we cloned the 5′-flanking region of the human ADAMTS4 gene and characterized its promoter activity by means of reporter assay using porcine chondrocytes and NIH3T3 cells. Reporter gene analysis using deletion variants suggested that the region between −383 and +10 relative to the tentative transcription start site is necessary for full promoter activity; this region contains one Sp1 and three AP2 sites. In addition, the segment between −726 and −384 appears to contain silencer element(s). A complete deletion mutant of the nuclear factor I (NFI) binding site at −441 to −429 resulted in recovery of the promoter activity in chondrocytes, but not in NIH3T3 cells. Thus, the NFI site is involved in negative regulation of the human ADAMTS4 promoter activity in chondrocytes.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1023/A:1007253930568

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1H NMR study of casein phosphopeptide (1-25): Assignment and conformation (1991)

Tsuda, Sakae ; Niki, Ryoya ; Kuwata, Tamotsu ; [et al.]

Chichester : Wiley-Blackwell

Organic Magnetic Resonance 29 (1991), S. 1097-1102

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ISSN: 0749-1581

Keywords: 1H NMR ; Casein phosphopeptide ; 2D NMR ; COSY ; HOHAHA ; NOESY ; β-Turn ; Chemistry ; Analytical Chemistry and Spectroscopy

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The solution conformation of β-casein phosphopeptide (CPP) was studied by 1H NMR spectroscopy. As a prerequisite to the conformational analysis the spectral assignment was carried out for CPP in the Ca2+-free and -bound states by the use of two-dimensional NMR spectroscopy. The assigned resonances were used for (1) pH-titration experiments, (2) elucidation of the temperature dependence of the amide resonance and (3) a nuclear Overhauser enhancement (NOE) experiment. Although the β-turn conformation is predicted for the sequence - Val8-Pro9-Gly10-Glu11-of CPP, the present NMR results do not provide favourable evidence for its formation.

Additional Material: 3 Ill.