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Reproduction (2007) 134 435-444
DOI: 10.1530/REP-06-0388
Copyright © 2007 Society for Reproduction and Fertility
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RESEARCH

Porcine sperm motility is regulated by serine phosphorylation of the glycogen synthase kinase-3{alpha}

I M Aparicio, M J Bragado, M C Gil, M Garcia-Herreros, L Gonzalez-Fernandez, J A Tapia and L J Garcia-Marin

Research Group of Intracellular Signalling and Technology of Reproduction, Faculty of Veterinary, University of Extremadura, 10071 Caceres, Spain

Correspondence should be addressed to L J Garcia-Marin who is now at Departamento de Fisiologia, Facultad de Veterinaria, Universidad de Extremadura, Avenida de la Universidad, s/n, 10071 Caceres, Spain; Email: ljgarcia{at}unex.es

Sperm functions are critically controlled through the phosphorylation state of specific proteins. Glycogen synthase kinase-3 (GSK3) is a serine/threonine kinase with two different isoforms ({alpha} and ß), the enzyme activity of which is inhibited by serine phosphorylation. Recent studies suggest that GSK3 is involved in the control of bovine sperm motility. Our aim was to investigate whether GSK3 is present in porcine spermatozoa and its role in the function of these cells. This work shows that both isoforms of GSK3 are present in whole cell lysates of porcine sperm and are phosphorylated on serine in spermatozoa stimulated with the cAMP analog, 8Br-cAMP. A parallel increase in serine phosphorylation of the isoform GSK3{alpha}, but not in the isoform GSK3ß, is observed after treatments that also induce a significant increase in porcine sperm velocity parameters. Therefore, a significant positive correlation among straight-line velocity, circular velocity, average velocity, rapid-speed spermatozoa, and GSK3{alpha} serine phosphorylation levels exists. Inhibition of GSK3 activity by alsterpaullone leads to a significant increase in the percentage of rapid- and medium-speed spermatozoa as well as in all sperm velocity parameters and coefficients. Moreover, pretreatment of porcine spermatozoa with alsterpaullone significantly increased the percentage of capacitated porcine spermatozoa and presents no effect in the number of acrosome-reacted porcine spermatozoa. Our work suggests that the isoform GSK3{alpha} plays a negative role in the regulation of porcine sperm motility and points out the possibility that sperm motile quality might be modulated according the activity state of GSK3{alpha}.




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