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Protein modification in the post-mating spermatophore of the signal crayfish Pacifastacus leniusculus: insight into the tyrosine phosphorylation in a non-motile spermatozoon
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SYSNO ASEP 0463432 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Protein modification in the post-mating spermatophore of the signal crayfish Pacifastacus leniusculus: insight into the tyrosine phosphorylation in a non-motile spermatozoon Author(s) Niksirat, H. (CZ)
Vancová, Marie (BC-A) RID, ORCID
Andersson, L. (SE)
James, P. (SE)
Kouba, A. (CZ)
Kozák, P. (CZ)Source Title Animal Reproduction Science. - : Elsevier - ISSN 0378-4320
Roč. 172, SEP (2016), s. 123-130Number of pages 8 s. Publication form Print - P Language eng - English Country NL - Netherlands Keywords microtubular radial arm ; spermatozoon capacitation ; tyrosine-phosphorylation ; ultrastructural localization Subject RIV EA - Cell Biology R&D Projects TE01020118 GA TA ČR - Technology Agency of the Czech Republic (TA ČR) Institutional support BC-A - RVO:60077344 UT WOS 000382411800014 EID SCOPUS 84990060958 DOI 10.1016/j.anireprosci.2016.07.009 Annotation After mating, spermatophores of signal crayfish are stored on the body of the female for a period before fertilization. This study compared the post-mating protein profile and pattern of protein tyrosine phosphorylation of the signal crayfish spermatophore to that of the freshly ejaculated spermatophore and found substantial differences. Two major bands of tyrosine-phosphorylated proteins of molecular weights 10 and 50 kDa were observed in the freshly ejaculated spermatophore of the signal crayfish. While the tyrosine-phosphorylated protein band with molecular weight 10 kDa was formed by protein(s) of similar pH, the band with molecular weight of 50 kDa consisted of proteins of varying pH. In the post mating spermatophore, the band with molecular weight of 50 kDa was not detected, and an increase in the level of protein tyrosine phosphorylation was observed in the 10 kDa band. The microtubular radial arms of the spermatozoon showed a positive reaction to an anti tyrosine antibody conjugated with gold particles in both the freshly ejaculated and post mating spermatophores. In conclusion, the male gamete of the signal crayfish undergoes molecular modification during post-mating storage on the body of the female including changes in the level of protein expression and protein tyrosine phosphorylation. Structural similarity of the radial arms in the crayfish immotile spermatozoon with flagellum, which is the main site of protein tyrosine phosphorylation in the mammalian motile spermatozoa, raises questions regarding evolution and function of such organelles across the animal kingdom that must be addressed in the future studies. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2017
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