Is the phosphorylation status of tyrosine proteins a marker for the cryo-capacitation of boar spermatozoa?

• Autorzy: Wysocki P , Koncicka K. , Strzezek J.
• Języki publikacji: EN

Abstrakty

EN

The phosphorylation of tyrosine protein residues in spermatozoa was dependent on the semen of individual boars at different stages of the cryopreservation technology. Sperm proteins in the fresh semen of a boar with poor semen freezability (boar K) exhibited a higher content of phosphotyrosine residues compared to boars with better semen freezability (boars F and J). In the semen samples extended in a Kortowo 3 extender (K3) and cooled at 16°C, there was a marked increase in protein phosphorylation in the sperm proteins of boars with good semen freezability. This was manifested in the appearance of phosphoproteins with molecular weights of 17, 32, 43, 52, 63 and 78 kDa. In the case of boar K, the cooled-storage of K3-extended semen at 5°C caused the extensive phosphorylation of sperm proteins, with molecular weights of 45, 65 i 100 kDa. A gradual reduction in sperm protein tyrosine phosphorylation was detected in the extender containing lipoprotein fraction isolated from ostrich egg yolk (LPFo) compared with the K3 extender, what has no protective substances. It might be suggested that seminal plasma acid phosphatases, especially the vesicular molecular form of acid phosphatase (PTAP), played a very important role in the regulation of tyrosine phosphorylation in boar sperm plasmalemma proteins. Differences were observed in the number of dephosphorylated proteins by different molecular forms of phosphatases. It was shown that phosphotyrosine residues in sperm proteins could be completely dephosphorylated by the vesicular PTAP. It seemed that only sperm phosphotyrosine proteins, with molecular weights of 17, 32, and 63 kDa, could be dephosphorylated by the epididymal molecular form of acid phosphatase.

Słowa kluczowe

EN

boar; semen; phosphorylation; phosphotyrosine; cryopreservation; tyrosine protein residue; spermatozoon; sperm protein; fresh semen; acid phosphatase; molecular form; seminal plasma

• Wydawca: -
• Czasopismo: Bulletin of the Veterinary Institute in Puławy
• Rocznik: 2009
• Tom: 53
• Numer: 2
• Opis fizyczny: p.229-232,fig.,ref.

Twórcy

autor

Wysocki P

• University of Warmia and Mazury in Olsztyn, 10-718 Olsztyn, Poland

autor

Koncicka K.

autor

Strzezek J.

Bibliografia

• 1. Bailey J.L., Bilodeau J.F., Cormier N.: Semen cryopreservation in domestic animals: a damaging and capacitating phenomenon. J Androl 2000, 21, 1-7.
• 2. Bravo M.M., Aparicio I.M., Garcia-Herreros M., Gil M.C., Peña F.J., Garcia-Marin L.J.: Changes in tyrosine phosphorylation associated with true capacitation and capacitation-like state in boar spermatozoa. Mol Reprod Dev 2005, 71, 88-96.
• 3. Ericsson S.A., Garner D.L., Thomas C.A., Downing T.W., Marshall C.E.: Interrelationship among fluorometric analyses of spermatozoal function, classical semen quality parameters and fertility of frozen-thawed bovine spermatozoa. Theriogenology 1993, 39, 1009- 1024.
• 4. Fraser L., Lecewicz M., Strzeżek J.: Fluorometric assessments of viability and mitochondrial status of boar spermatozoa following liquid storage. Pol J Vet Sci 2002, 5, 85-92.
• 5. Garner D.L., Pinkel D., Johnson L.A., Pace M.M.: Assesment of spermatozoa function using dual fluorescent staining and flow cytometric analyses. Biol Reprod 1986, 34, 127-138.
• 6. Kaneto M., Harayama H., Miyake M., Kato S.: Capacitation -like alternations in cooled boar spermatozoa: assessment by the chlortetracycline staining assay and immunodetection of tyrosine-phosphorylated sperm proteins. Anim Reprod Sci 2002, 73, 197-209.
• 7. Laemmli U.K.: Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 1970, 277, 680-685.
• 8. Perez-Pe R., Grasa P., Fernandez-Juan M., Peleato M.L., Cebrian-Perez J.A., Muino-Blanco T.: Seminal plasma proteins reduce protein tyrosine phosphorylation in the plasma membrane of cold-shocked ram spermatozoa. Mol Reprod Dev 2002, 61, 226-233.
• 9. Strzeżek J., Glogowski J., Hopfer E., Wojtkiewicz K.: „Kortowska” method of freezing boar semen. Medycyna Wet 1985 41, 349-353.
• 10. Strzeżek J., Lecewicz M., Dziekońska A., Fraser L.: A simple method of extraction of lipoprotein fractions from avian egg yolk - protective effect on cooled boar semen. Proceedings of the 5th International Conference on Boar Semen Preservation, Doorwerth, The Netherlands, Theriogenology 2003, 6, 690-691.
• 11. Tomes C.N., Carballada R., Moses D.F., Katz D.F., Saling P.M.: Treatment of human spermatozoa with seminal plasma inhibits protein tyrosine phosphorylation. Mol Hum Reprod 1998, 4, 17-25.
• 12. Urner F., Sakkas D.: Protein phosphorylation in mammalian spermatozoa. Reproduction 2003, 125, 17-26.
• 13. Vadnais M.L., Kirkwood R.N., Sprecher D.J., Chou K.: Effect of extender, incubation temperature and added seminal plasma on capacitation of cryopreserved thawed boar sperm as determined by chlortetracycline staining. Anim Reprod Sci 2005, 90, 347-354.
• 14. Vadnais M.L., Roberts K.P.: Effects of seminal plasma on cooling-induced capacitative changes in boar sperm. J Androl 2007, 28, 416-422.
• 15. Wysocki P., Lecewicz A., Strzeżek J.: Phosphorylation status of boar spermatozoa proteins during liquid storage at 5°C and 16°C. Acta Biochim Pol 2006, 53, 516.
• 16. Wysocki P., Strzezek J.: Isolation and biochemical characteristics of a molecular form of epididymal acid phosphatase of boar seminal plasma. Theriogenology 2006, 66, 2152-2159.
• 17. Wysocki P., Strzezek J.: Purification and characterization of a protein tyrosine acid phosphatase from boar seminal vesicle glands. Theriogenology 2003, 59, 1011-1025.