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The role of Ca2+ and Na+ membrane transport in brook trout (Salvelinus fontinalis) spermatozoa motility

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The role of environmental ion composition and osmolality in Ca2+ signaled activation was assessed in spermatozoa of brook trout Salvelinus fontinalis. Milt from ten mature males was obtained by abdominal massage. Spermatozoa motility was evaluated in 0, 100, and 300 mOsm/kg NaCl or sucrose solutions, buffered by 10 mM Tris–HCl pH 8.5. For investigation of spermatozoa reaction to external Ca2+ concentration, 2 mM ethylene glycol tetraacetic acid (EGTA) was added to the activation media as a calcium ions chelator. For investigation of the effect of external Na+ concentration in conditions of low external Ca2+, 100 µM amiloride was added to the EGTA-containing solutions as a Na+ transport blocker. Low motility was observed in sucrose (Na+ free) solutions containing 2 mM EGTA but not in Na+ solutions containing 2 mM EGTA. Addition of amiloride led to significantly increased motility (P < 0.05) compared with sucrose (Na+ free) solutions containing 2 mM EGTA. We conclude that Na+ transport in Ca2+-free solutions plays a regulatory role in brook trout spermatozoa activation. The influence of competitive Na+ and Ca2+ transport on the control of spermatozoa activation requires further study with respect to its application for improvement of artificial activation and storage media.

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Acknowledgments

We are grateful to Lucidus Consultancy, UK for English correction and suggestions. This work was supported by several research grants such as CENAKVA CZ.1.05/2.1.00/01.0024, strengthening of excellence scientific teams in USB FFPW CZ.1.07/2.3.00/20.0024, GAJU 114/2013/Z, GAJU 123/2014/Z, GACR P502/11/0090, and GACR P502/12/1973. The results of the project LO1205 were obtained with a financial support from the MEYS of the CR under the NPU I program.

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Correspondence to Olga Bondarenko.

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Bondarenko, O., Dzyuba, B., Cosson, J. et al. The role of Ca2+ and Na+ membrane transport in brook trout (Salvelinus fontinalis) spermatozoa motility. Fish Physiol Biochem 40, 1417–1421 (2014). https://doi.org/10.1007/s10695-014-9936-5

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