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Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor.

Chen, Y.; Cann, M.J.; Litvin, T.N.; Iourgenko, V.; Sinclair, M.L.; Levin, L.R.; Buck, J.


Y. Chen

T.N. Litvin

V. Iourgenko

M.L. Sinclair

L.R. Levin

J. Buck


Spermatozoa undergo a poorly understood activation process induced by bicarbonate and mediated by cyclic adenosine 3′,5′-monophosphate (cAMP). It has been assumed that bicarbonate mediates its effects through changes in intracellular pH or membrane potential; however, we demonstrate here that bicarbonate directly stimulates mammalian soluble adenylyl cyclase (sAC) activity in vivo and in vitro in a pH-independent manner. sAC is most similar to adenylyl cyclases from cyanobacteria, and bicarbonate regulation of cyclase activity is conserved in these early forms of life. sAC is also expressed in other bicarbonate-responsive tissues, which suggests that bicarbonate regulation of cAMP signaling plays a fundamental role in many biological systems.


Chen, Y., Cann, M., Litvin, T., Iourgenko, V., Sinclair, M., Levin, L., & Buck, J. (2000). Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor. Science, 289(5479), 625-628.

Journal Article Type Article
Publication Date 2000-07
Journal Science
Print ISSN 0036-8075
Electronic ISSN 1095-9203
Publisher American Association for the Advancement of Science
Peer Reviewed Peer Reviewed
Volume 289
Issue 5479
Pages 625-628
Public URL