IndraLab

Statements


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"These data confirm that STAT1 DNA binding ability is not disrupted by adenosine treatment."

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"Furthermore, these results suggest that adenosine does not impede STAT1 dimerization because only the stable dimer is capable of subcellular localization to the nucleus and binding DNA."

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"We observed similar inhibition of STAT1 S727 phosphorylation in cells treated with A 1, A 2A, and A 2B receptor specific antagonists (CPX, SCH 58261, and alloxazine, respectively), suggesting that these three receptor subtypes do not play an important role in adenosine mediated STAT1 deactivation (XREF_FIG)."

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"Our data suggest that adenosine blocks IFN-gamma-induced STAT1 transcriptional activity, providing a functional correlate for its effect on phosphorylation of STAT1 at S727."

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"In contrast, we show that adenosine treatment both delays STAT1 responsive promoter activity and markedly attenuates the maximal STAT1 activity in IFN-gamma-stimulated macrophages, providing a functional correlate to the reduction in STAT1 S727 phosphorylation observed in adenosine treated cells."