Protein phosphorylation in spermatozoa motility of Acipenser ruthenus and Cyprinus carpio

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F17%3A43895530" target="_blank" >RIV/60076658:12520/17:43895530 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1530/REP-16-0662" target="_blank" >http://dx.doi.org/10.1530/REP-16-0662</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1530/REP-16-0662" target="_blank" >10.1530/REP-16-0662</a>

Result language

angličtina

Original language name

Protein phosphorylation in spermatozoa motility of Acipenser ruthenus and Cyprinus carpio

Original language description

Spermatozoa of externally fertilizing freshwater fish possess several different modes of motility activation. Spermatozoa of common carp (Cyprinus carpio L.) are activated by hypoosmolality, whereas spermatozoa of sterlet (Acipenser ruthenus) require Ca2+ and low concentration of K+ for motility activation. Intracellular signaling differs between these two species as well, particularly in terms of utilization of secondary messengers (cAMP and Ca2+), and kinase activities. The current study was performed in order to determine the importance of protein phosphorylation and protein kinases for activation of sperm motility in carp and sterlet. Treatment with kinase inhibitors indicates that protein kinases A and C (PKA and PKC) participate in spermatozoa motility of both species. Immunodetection of phospho-(Ser/Thr) PKA substrates shows that phosphorylated proteins are localized differently in spermatozoa of carp and sterlet. Strong phosphorylation of PKC substrate was observed in flagella of sterlet spermatozoa, whereas in carp sperm, PKC substrates were lightly phosphorylated in the midpiece and flagella. Motility activation induced either phosphorylation or dephosphorylation on serine, threonine and tyrosine residues of numerous proteins in carp and sterlet spermatozoa. Proteomic methods were used to identify proteins whose phosphorylation state changes upon the initiation of sperm motility. Numerous mitochondrial and glycolytic enzymes were identified in spermatozoa of both species, as well as axonemal proteins, heat shock proteins, septins and calcium-binding proteins. Our results contribute to an understanding of the roles of signaling molecules, protein kinases and protein phosphorylation in motility activation and regulation of two valuable fish species, C. carpio and A. ruthenus.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

30105 - Physiology (including cytology)

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2017

Confidentiality

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

Name of the periodical

Reproduction

ISSN

1470-1626

e-ISSN

—

Volume of the periodical

154

Issue of the periodical within the volume

5

Country of publishing house

GB - UNITED KINGDOM

Number of pages

21

Pages from-to

653-673

UT code for WoS article

000414160000017

EID of the result in the Scopus database

2-s2.0-85030777446