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Soluble Adenylyl Cyclase as an Evolutionarily Conserved Bicarbonate Sensor

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 bicarb...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2000-07, Vol.289 (5479), p.625-628
Main Authors: Chen, Yanqiu, Cann, Martin J., Litvin, Tatiana N., Iourgenko, Vadim, Sinclair, Meeghan L., Levin, Lonny R., Buck, Jochen
Format: Article
Language:English
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.289.5479.625