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1 Ciencias Fisiologicas, Pontificia Universidad Catolica de Chile, Santiago, Chile
2 Biologia, Universidad de Santiago de Chile, Santiago, Chile
* To whom correspondence should be addressed. E-mail: mvilla{at}bio.puc.cl.
An increase in intracellular free Ca2+ concentration ([Ca2+]i) has been shown to be involved in the increase in ciliary beat frequency (CBF) in response to ATP; however the signalling pathways associated with the Ins (1,4,5)-P3 (IP3) receptor dependent Ca2+ mobilization remain unresolved. Using radioimmunoassay techniques, we demonstrated the appearance of two IP3 peaks, occurring at 10 and 60 s after ATP addition, which strongly correlated with a release of intracellular Ca2+ from internal stores and an influx of extracellular Ca2+, respectively. In addition, the ATP dependent Ca2+ mobilization required protein kinase C (PKC) and Ca2+/calmodulin-dependent protein kinase II (CaMKII) activation. We found an increase in PKC activity in response to ATP, with a peak at 60 s after ATP addition. Xestospongin C, a IP3 receptor blocker, significantly diminished both the ATP induced increase in CBF and the initial transient [Ca2+]i component. ATP addition in the presence of xestospongin C or thapsigargin revealed that the Ca2+ influx is also dependent on IP3 receptor activation. Immunofluorescence and confocal microscopy studies showed the presence of IP3 receptor types 1 and 3 in cultured ciliated cells. Immunogold electron microscopy localized IP3 receptor type 3 to the nucleus, the endoplasmic reticulum and interestingly, to the plasma membrane. In contrast, IP3 receptor type 1 was found exclusively in the nucleus and the endoplasmic reticulum. Our study demonstrates for the first time the presence of IP3 receptor type 3 in the plasma membrane in ciliated cells, and leads us to postulate that the IP3 receptor can directly trigger a Ca2+ influx in response to ATP.
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