Adenophostin A can stimulate Ca2+ influx without depleting the inositol 1,4,5-trisphosphate-sensitive Ca2+ stores in the Xenopus oocyte.

@article{Delisle1997AdenophostinAC,
  title={Adenophostin A can stimulate Ca2+ influx without depleting the inositol 1,4,5-trisphosphate-sensitive Ca2+ stores in the Xenopus oocyte.},
  author={Susan Delisle and E W Marksberry and C D Bonnett and David J Jenkins and Barry V. L. Potter and Miyoko Takahashi and Kazuhiko Tanzawa},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 15},
  pages={9956-61}
}
Adenophostin A possesses the highest known affinity for the inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) receptor (InsP3R). The compound shares with Ins(1,4,5)P3 those structural elements essential for binding to the InsP3R. However, its adenosine 2'-phosphate moiety has no counterpart in the Ins(1,4,5)P3 molecule. To determine whether its unique structure conferred a distinctive biological activity, we characterized the adenophostin-induced Ca2+ signal in Xenopus oocytes using the Ca2+-gated Cl… CONTINUE READING