3D in situ imaging of the female reproductive tract reveals molecular signatures of fertilizing spermatozoa in mice
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F20%3A00541406" target="_blank" >RIV/86652036:_____/20:00541406 - isvavai.cz</a>
Výsledek na webu
<a href="https://elifesciences.org/articles/62043" target="_blank" >https://elifesciences.org/articles/62043</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.7554/eLife.62043" target="_blank" >10.7554/eLife.62043</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
3D in situ imaging of the female reproductive tract reveals molecular signatures of fertilizing spermatozoa in mice
Popis výsledku v původním jazyce
Out of millions of ejaculated sperm, a few reach the fertilization site in mammals. Flagellar Ca2+ signaling nanodomains, organized by multi-subunit CatSper calcium channel complexes, are pivotal for sperm migration in the female tract, implicating CatSper-dependent mechanisms in sperm selection. Here using biochemical and pharmacological studies, we demonstrate that CatSper1 is an O-linked glycosylated protein, undergoing capacitation-induced processing dependent on Ca2+ and phosphorylation cascades. CatSper1 processing correlates with protein tyrosine phosphorylation (pY) development in sperm cells capacitated in vitro and in vivo. Using 3D in situ molecular imaging and ANN-based automatic detection of sperm distributed along the cleared female tract, we demonstrate that spermatozoa past the utero-tubal junction possess the intact CatSper1 signals. Together, we reveal that fertilizing mouse spermatozoa in situ are characterized by intact CatSper channel, lack of pY, and reacted acrosomes. These findings provide molecular insight into sperm selection for successful fertilization in the female reproductive tract.
Název v anglickém jazyce
3D in situ imaging of the female reproductive tract reveals molecular signatures of fertilizing spermatozoa in mice
Popis výsledku anglicky
Out of millions of ejaculated sperm, a few reach the fertilization site in mammals. Flagellar Ca2+ signaling nanodomains, organized by multi-subunit CatSper calcium channel complexes, are pivotal for sperm migration in the female tract, implicating CatSper-dependent mechanisms in sperm selection. Here using biochemical and pharmacological studies, we demonstrate that CatSper1 is an O-linked glycosylated protein, undergoing capacitation-induced processing dependent on Ca2+ and phosphorylation cascades. CatSper1 processing correlates with protein tyrosine phosphorylation (pY) development in sperm cells capacitated in vitro and in vivo. Using 3D in situ molecular imaging and ANN-based automatic detection of sperm distributed along the cleared female tract, we demonstrate that spermatozoa past the utero-tubal junction possess the intact CatSper1 signals. Together, we reveal that fertilizing mouse spermatozoa in situ are characterized by intact CatSper channel, lack of pY, and reacted acrosomes. These findings provide molecular insight into sperm selection for successful fertilization in the female reproductive tract.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10602 - Biology (theoretical, mathematical, thermal, cryobiology, biological rhythm), Evolutionary biology
Návaznosti výsledku
Projekt
<a href="/cs/project/GJ20-17403Y" target="_blank" >GJ20-17403Y: Vliv estrogenů na epigenom testes/spermií a časný vývoj zárodku</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2020
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
eLife
ISSN
2050-084X
e-ISSN
—
Svazek periodika
9
Číslo periodika v rámci svazku
OCT 20 2020
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
29
Strana od-do
e62043
Kód UT WoS článku
000595597500001
EID výsledku v databázi Scopus
2-s2.0-85095704918