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(biochemistry) purine base found in DNA and RNA; pairs with thymine in DNA and with uracil in RNA (同)A

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アデニン(肝臓・茶の葉から採れる塩基の一種)

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English Journal

Extracellular β-NAD(+) inhibits interleukin-1-induced matrix metalloproteinase-1 and -3 expression on human gingival fibroblasts.

Gotoh K1, Nemoto E, Kanaya S, Shimauchi H.Author information 1Division of Periodontology and Endodontology, Tohoku University Graduate School of Dentistry, Sendai, Japan.AbstractThere is increasing evidence to show that extracellular β-nicotinamide adenine dinucleotide (β-NAD(+)) modulates various biological functions in inflammatory/immune regions. The aim of this study was to determine the effect of β-NAD(+) on matrix metalloproteinase (MMP) expression on human gingival fibroblasts (hGF), the excess production of which leads to the matrix degradation associated with the pathological processes of periodontitis. The expression of MMP-1 and MMP-3 on hGF was determined by real-time polymerase chain reaction (PCR) and an enzyme-linked immunosorbent assay. The phosphorylated status of mitogen-activated protein (MAP) kinases, extracellular signal-regulated kinase 1/2 (ERK), c-Jun N-terminal kinase (JNK), and p38 and the expression of inhibitor κB (IκB)α were determined by Western blotting. β-NAD(+) inhibited the expression of MMP-1 and MMP-3 triggered by IL-1α at gene and protein levels. β-NAD(+) had no significant effect on the IL-1α-induced phosphorylation of ERK1/2, JNK, and p38 and also had no effect on the IL-1α-induced degradation of IκBα relative to the control, suggesting that inhibition by β-NAD(+) was independent of the MAP kinase and the nuclear factor-κB signaling pathways. Transcripts of NAD(+)-metabolizing enzymes, such as NAD(+)-glycohydrolase, adenosine diphosphate (ADP)-ribosylcyclase, and ADP-ribosyltransferase, were expressed by hGF as assessed by RT-PCR. Experiments using α-NAD(+), which is not a substrate for ADP-ribosylcyclase or ADP-ribosyltransferase, revealed the possible contribution of NAD(+)-glycohydrolase to the inhibition of MMP. This is consistent with the finding that ADP-ribose, an NAD(+)-metabolite by NAD(+)-glycohydrolase, exhibited MMP inhibition similar to β-NAD(+). The present findings may provide an additional viewpoint to clarify a natural feedback mechanism during the inflammatory process in periodontal tissue.
Connective tissue research.Connect Tissue Res.2013;54(3):204-9. doi: 10.3109/03008207.2013.782013. Epub 2013 Apr 15.
There is increasing evidence to show that extracellular β-nicotinamide adenine dinucleotide (β-NAD(+)) modulates various biological functions in inflammatory/immune regions. The aim of this study was to determine the effect of β-NAD(+) on matrix metalloproteinase (MMP) expression on human gingiva
PMID 23509928