Precision Structural Interpretation of Site-Specific N-Glycans in Seminal Plasma
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F22%3A43904568" target="_blank" >RIV/60076658:12520/22:43904568 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1021/acs.jproteome.2c00046" target="_blank" >https://doi.org/10.1021/acs.jproteome.2c00046</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jproteome.2c00046" target="_blank" >10.1021/acs.jproteome.2c00046</a>
Alternative languages
Result language
angličtina
Original language name
Precision Structural Interpretation of Site-Specific N-Glycans in Seminal Plasma
Original language description
N-Linked glycoproteins are rich in seminal plasma, playing various essential roles in supporting sperm function and the fertilization process. However, the detailed information on these glycoproteins, particularly site-specific glycan structures, is still limited. In this study, a precision site-specific N-glycoproteome map of human seminal plasma was established by employing the site-specific glycoproteomic approach and a recently developed glycan structure interpretation software, StrucGP. A total of 9567 unique glycopeptides identified in human seminal plasma were composed of 773 N-linked glycan structures and 1019 N-glycosites from 620 glycoproteins. These glycans were comprised of four types of core structures and 13 branch structures. The majority of identified glycoproteins functioned in response to stimulus and immunity. As we reported in human spermatozoa, heavy fucosylation (fucose residues >= 6 per glycan) was also detected on seminal plasma glycoproteins such as clusterin and galectin-3-binding protein, which were involved in the immune response of biological processes and reactome pathways. Comparison of site-specific glycans between seminal plasma and spermatozoa revealed more complicated glycan structures in seminal plasma than in spermatozoa, even on their shared glycoproteins. These present data will be greatly beneficial for the in-depth structural and functional study of glycosylation in the male reproduction system.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
30405 - Medical biotechnology related ethics
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Proteome Research
ISSN
1535-3893
e-ISSN
1535-3907
Volume of the periodical
21
Issue of the periodical within the volume
neuvedeno
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
nestrankovano
UT code for WoS article
000818959500001
EID of the result in the Scopus database
2-s2.0-85131697246