Protein modification in the post-mating spermatophore of the signal crayfish Pacifastacus leniusculus: insight into the tyrosine phosphorylation in a non-motile spermatozoon

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F16%3A43890475" target="_blank" >RIV/60076658:12520/16:43890475 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60077344:_____/16:00463432 RIV/60076658:12310/16:43890475

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S0378432016302834" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0378432016302834</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.anireprosci.2016.07.009" target="_blank" >10.1016/j.anireprosci.2016.07.009</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Protein modification in the post-mating spermatophore of the signal crayfish Pacifastacus leniusculus: insight into the tyrosine phosphorylation in a non-motile spermatozoon

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Protein modification in the post-mating spermatophore of the signal crayfish Pacifastacus leniusculus: insight into the tyrosine phosphorylation in a non-motile spermatozoon

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Animal Reproduction Science

ISSN

0378-4320

e-ISSN

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Svazek periodika

172

Číslo periodika v rámci svazku

September

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

123-130

Kód UT WoS článku

000382411800014

EID výsledku v databázi Scopus

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