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Recently, CaM has been shown to bind to Fas, which is regulated during Fas or CaM antagonist\u2010mediated apoptosis in Jurkat cells and osteoclasts. Accordingly, the present studies were designed to determine whether Fas interacts with CaM in cholangiocarcinoma cells and to elucidate its role in regulating Fas\u2010mediated apoptosis. CaM bound to Fas in cholangiocarcinoma cells. CaM was identified in the Fas\u2010mediated death inducing signaling complex (DISC). The amount of CaM recruited into the DISC was increased after Fas\u2010stimulation, a finding confirmed by immunofluorescent analysis that demonstrated increased membrane co\u2010localization of CaM and Fas upon Fas\u2010stimulation. Consistently, increased Fas microaggregates in response to Fas\u2010stimulation were found to bind to CaM. Fas\u2010induced recruitment of CaM into the DISC was inhibited by the Ca<jats:sup>2+<\/jats:sup>chelator, EGTA, and the CaM antagonist, trifluoperazine (TFP). TFP decreased DISC\u2010induced cleavage of caspase\u20108. Further, inhibition of actin polymerization, which has been demonstrated to abolish DISC formation, inhibited the recruitment of CaM into the DISC. These results suggest an important role of CaM in mediating DISC formation, thus regulating Fas\u2010mediated apoptosis in cholangiocarcinoma cells. Characterization of the role of CaM in Fas\u2010mediated DISC formation and apoptosis signaling may provide important insights in the development of novel therapeutic targets for cholangiocarcinoma. J. Cell. Biochem. 103: 788\u2013799, 2008. \u00a9 2007 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jcb.21447","type":"journal-article","created":{"date-parts":[[2007,7,24]],"date-time":"2007-07-24T15:49:05Z","timestamp":1185292145000},"page":"788-799","source":"Crossref","is-referenced-by-count":29,"title":["Calmodulin binding to the Fas\u2010Mediated death\u2010inducing signaling complex in cholangiocarcinoma 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