Characterization of cAMP ‐phosphodiesterase activity in bovine seminal plasma
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· 2016
· Open Access
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· DOI: https://doi.org/10.1111/andr.12267
· OA: W2507565214
Summary The second messenger cyclic adenosine monophosphate ( cAMP ) has a central role in sperm physiology. Extracellular cAMP can be sequentially degraded into 5′ AMP and adenosine by ecto‐phosphodiesterases (ecto‐ PDE ) and ecto‐nucleotidases, a phenomenon called extracellular cAMP ‐adenosine pathway. As cAMP ‐adenosine pathway is involved in sperm capacitation, we hypothesize that extracellular PDE s are functionally present in seminal plasma. Exclusively measuring cAMP ‐ PDE activity, total activity in bovine seminal plasma was 10.1 ± 1.5 fmoles/min/μg. Using different family‐specific PDE inhibitors, we showed that in seminal plasma, the major cAMP ‐ PDE activity was papaverine sensitive (47.5%). These data support the presence of PDE 10 in bovine seminal plasma and was further confirmed by western blot. In epididymal fluid, total cAMP ‐ PDE activity was 48.2 ± 14.8 fmoles/min/μg and we showed that the major cAMP ‐ PDE activity was 3‐isobutyl‐methylxanthine insensitive and thus ascribed to PDE 8 family. PDE 10A mRNA s were found in the testis, epididymis, and seminal vesicles. cAMP ‐ PDE activity is present in bovine seminal plasma and epididymal fluid. The results suggest a role for ecto‐ PDE s present in those fluids in the signaling pathways involved in sperm functions.
