Structural and site-specific characterization of distinctiveNglycans with heavy fucosylation in human semen

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F25%3A43910164" target="_blank" >RIV/60076658:12520/25:43910164 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1016/j.carpta.2025.100941" target="_blank" >https://doi.org/10.1016/j.carpta.2025.100941</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.carpta.2025.100941" target="_blank" >10.1016/j.carpta.2025.100941</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural and site-specific characterization of distinctiveNglycans with heavy fucosylation in human semen

Popis výsledku v původním jazyce

Heavy fucosylation (fucose residues &gt;= 6 per glycan) has been previously reported in human semen with unclear precise site-specific glycan structures. In current study, we characterized heavily fucosylated glycoproteins as a distinctive feature of human spermatozoa (HS) and seminal plasma (HSP), with a precise definition of glycan structural features at the glycosite-specific level. There were 49 unique heavily fucosylated intact glycopeptides (IGPs) at 15 N-glycosites from 12 glycoproteins identified in HS, and 188 unique heavily fucosylated IGPs at 58 N-glycosites from 37 glycoproteins in HSP. Among these heavily fucosylated glycoproteins, 10 were shared in HS and HSP, 2 were detected only in HS and 17 only in HSP. Almost all heavily fucosylated glycans were complex Nglycans with core fucosylation and Lewis antennary, among which CLU were glycosylated by ten and nine fucoses per glycan in HS and HSP, respectively. Moreover, these heavily fucosylated glycans varied from tri- to hexa-antennas. Notably, the N-glycan structures on shared heavily fucosylated glycoproteins were more complex in HSP than in HS. These heavily fucosylated glycoproteins identified in human semen represent a valuable and distinctive resource for glycopeptide studies, offering significant potential for advancing glycoproteomic methodologies and clinical research into male infertility.

Název v anglickém jazyce

Structural and site-specific characterization of distinctiveNglycans with heavy fucosylation in human semen

Popis výsledku anglicky

Heavy fucosylation (fucose residues &gt;= 6 per glycan) has been previously reported in human semen with unclear precise site-specific glycan structures. In current study, we characterized heavily fucosylated glycoproteins as a distinctive feature of human spermatozoa (HS) and seminal plasma (HSP), with a precise definition of glycan structural features at the glycosite-specific level. There were 49 unique heavily fucosylated intact glycopeptides (IGPs) at 15 N-glycosites from 12 glycoproteins identified in HS, and 188 unique heavily fucosylated IGPs at 58 N-glycosites from 37 glycoproteins in HSP. Among these heavily fucosylated glycoproteins, 10 were shared in HS and HSP, 2 were detected only in HS and 17 only in HSP. Almost all heavily fucosylated glycans were complex Nglycans with core fucosylation and Lewis antennary, among which CLU were glycosylated by ten and nine fucoses per glycan in HS and HSP, respectively. Moreover, these heavily fucosylated glycans varied from tri- to hexa-antennas. Notably, the N-glycan structures on shared heavily fucosylated glycoproteins were more complex in HSP than in HS. These heavily fucosylated glycoproteins identified in human semen represent a valuable and distinctive resource for glycopeptide studies, offering significant potential for advancing glycoproteomic methodologies and clinical research into male infertility.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10601 - Cell biology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

Carbohydrate Polymer Technologies and Applications

ISSN

2666-8939

e-ISSN

2666-8939

Svazek periodika

11

Číslo periodika v rámci svazku

neuvedeno

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

nestránkováno

Kód UT WoS článku

001539168300001

EID výsledku v databázi Scopus

2-s2.0-105010588191