Complexity and modification of the bull sperm glycocalyx during epididymal maturation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F24%3A00586446" target="_blank" >RIV/86652036:_____/24:00586446 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60460709:41210/24:98491

Výsledek na webu

<a href="https://faseb.onlinelibrary.wiley.com/doi/epdf/10.1096/fj.202400551RR" target="_blank" >https://faseb.onlinelibrary.wiley.com/doi/epdf/10.1096/fj.202400551RR</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1096/fj.202400551RR" target="_blank" >10.1096/fj.202400551RR</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Complexity and modification of the bull sperm glycocalyx during epididymal maturation

Popis výsledku v původním jazyce

Mammalian spermatozoa have a surface covered with glycocalyx, consisting of heterogeneous glycoproteins and glycolipids. This complexity arises from diverse monosaccharides, distinct linkages, various isomeric glycans, branching levels, and saccharide sequences. The glycocalyx is synthesized by spermatozoa developing in the testis, and its subsequent alterations during their transit through the epididymis are a critical process for the sperm acquisition of fertilizing ability. In this study, we performed detailed analysis of the glycocalyx on the sperm surface of bull spermatozoa in relation to individual parts of the epididymis using a wide range (24) of lectins with specific carbohydrate binding preferences. Fluorescence analysis of intact sperm isolated from the bull epididymides was complemented by Western blot detection of protein extracts from the sperm plasma membrane fractions. Our experimental results revealed predominant sequential modification of bull sperm glycans with N-acetyllactosamine (LacNAc), followed by subsequent sialylation and fucosylation in a highly specific manner. Additionally, variations in the lectin detection on the sperm surface may indicate the acquisition or release of glycans or glycoproteins. Our study is the first to provide a complex analysis of the bull sperm glycocalyx modification during epididymal maturation.

Název v anglickém jazyce

Complexity and modification of the bull sperm glycocalyx during epididymal maturation

Popis výsledku anglicky

Mammalian spermatozoa have a surface covered with glycocalyx, consisting of heterogeneous glycoproteins and glycolipids. This complexity arises from diverse monosaccharides, distinct linkages, various isomeric glycans, branching levels, and saccharide sequences. The glycocalyx is synthesized by spermatozoa developing in the testis, and its subsequent alterations during their transit through the epididymis are a critical process for the sperm acquisition of fertilizing ability. In this study, we performed detailed analysis of the glycocalyx on the sperm surface of bull spermatozoa in relation to individual parts of the epididymis using a wide range (24) of lectins with specific carbohydrate binding preferences. Fluorescence analysis of intact sperm isolated from the bull epididymides was complemented by Western blot detection of protein extracts from the sperm plasma membrane fractions. Our experimental results revealed predominant sequential modification of bull sperm glycans with N-acetyllactosamine (LacNAc), followed by subsequent sialylation and fucosylation in a highly specific manner. Additionally, variations in the lectin detection on the sperm surface may indicate the acquisition or release of glycans or glycoproteins. Our study is the first to provide a complex analysis of the bull sperm glycocalyx modification during epididymal maturation.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA22-31156S" target="_blank" >GA22-31156S: Klíčové molekuly zapojené do maturace gamet a vazby spermií se zona pellucida u prasat a skotu</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

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

Název periodika

FASEB Journal

ISSN

0892-6638

e-ISSN

1530-6860

Svazek periodika

38

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

23

Strana od-do

e23687

Kód UT WoS článku

001230210500001

EID výsledku v databázi Scopus

2-s2.0-85194127693