TY - JOUR
T1 - Modulation of AP-1 activity by nitric oxide (NO) in vitro
T2 - NO-mediated modulation of AP-1
AU - Tabuchi, Akiko
AU - Sano, Kuniaki
AU - Oh, Esther
AU - Tsuchiya, Tomofusa
AU - Tsuda, Masaaki
PY - 1994/8/29
Y1 - 1994/8/29
N2 - To understand the role of nitric oxide (NO) in controlling the specific DNA-binding activities of transcriptional factors, we investigated the in vitro effect of the NO-donor sodium nitroprusside (SNP) on the AP-1 activity of cultured mouse cerebellar granule cells. A gel-mobility assay showed that SNP inhibited AP-1 activity in the presence, but not the absence of dithiothreitol (DTT). This DTT-dependent inhibition of AP-1 activity by SNP corresponded with the activation of the chemical reactivity of SNP with DTT, which can be monitored by the production of nitrite (NO-2). In contrast, diamide, a typical sulfhydryl oxidizing agent, inhibited AP-1 activity in the absence of DTT and its inhibitory effect was reversed competitively by DTT. Studies using structurally or functionally related analogues of SNP demonstrated that S-nitrosylation of the AP-1 moiety mediated by some NO-carriers but not by free NO, which can be produced by the chemical reaction of SNP with DTT, was responsible for the inhibition of AP-1 activity, suggesting NO-mediated regulation of the AP-1 transcriptional factor.
AB - To understand the role of nitric oxide (NO) in controlling the specific DNA-binding activities of transcriptional factors, we investigated the in vitro effect of the NO-donor sodium nitroprusside (SNP) on the AP-1 activity of cultured mouse cerebellar granule cells. A gel-mobility assay showed that SNP inhibited AP-1 activity in the presence, but not the absence of dithiothreitol (DTT). This DTT-dependent inhibition of AP-1 activity by SNP corresponded with the activation of the chemical reactivity of SNP with DTT, which can be monitored by the production of nitrite (NO-2). In contrast, diamide, a typical sulfhydryl oxidizing agent, inhibited AP-1 activity in the absence of DTT and its inhibitory effect was reversed competitively by DTT. Studies using structurally or functionally related analogues of SNP demonstrated that S-nitrosylation of the AP-1 moiety mediated by some NO-carriers but not by free NO, which can be produced by the chemical reaction of SNP with DTT, was responsible for the inhibition of AP-1 activity, suggesting NO-mediated regulation of the AP-1 transcriptional factor.
KW - Nitric oxide (NO) AP-1
KW - Redox regulation
KW - S-nitrosylation
KW - Sodium nitroprusside (SNP)
KW - Transcriptional factor
UR - http://www.scopus.com/inward/record.url?scp=0028146764&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(94)00839-6
DO - 10.1016/0014-5793(94)00839-6
M3 - 学術論文
C2 - 8076680
AN - SCOPUS:0028146764
SN - 0014-5793
VL - 351
SP - 123
EP - 127
JO - FEBS Letters
JF - FEBS Letters
IS - 1
ER -