Biological Functions and Large-Scale Profiling of Protein Glycosylation in Human Semen
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F20%3A43901034" target="_blank" >RIV/60076658:12520/20:43901034 - isvavai.cz</a>
Result on the web
<a href="https://pubs.acs.org/doi/full/10.1021/acs.jproteome.9b00795" target="_blank" >https://pubs.acs.org/doi/full/10.1021/acs.jproteome.9b00795</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jproteome.9b00795" target="_blank" >10.1021/acs.jproteome.9b00795</a>
Alternative languages
Result language
angličtina
Original language name
Biological Functions and Large-Scale Profiling of Protein Glycosylation in Human Semen
Original language description
Glycosylation is one of the most important post-translational modifications of proteins and plays an essential role in spermatogenesis, maturation, extracellular quality control, capacitation, sperm-egg recognition, and final fertilization. Spermatozoa are synthesized in the testes inactively with a thick glycocalyx and passed through the epididymis for further modification by glycosylation, deglycosylation, and integration to reach maturation. Subsequently, sperm capacitation and further fertilization require redistribution of glycoconjugates and dramatic glycocalyx modification of the spermatozoa surface. Furthermore, glycoproteins and glycans in seminal plasma are functional in maintaining spermatozoa structure and stability. Therefore, aberrant glycosylation may cause alteration of semen function and even infertility. Currently, mass spectrometry-based technologies have allowed large-scale profiling of glycans and glycoproteins in human semen. Quantitative analysis of semen glycosylation has also indicated many involved glycoproteome issues in male infertility and the potential biomarkers for diagnosis of male infertility in clinical. This review summarizes the role of glycosylation during spermatozoa development, the large-scale profiling of glycome and glycoproteome in human semen, as well as the association of aberrant glycosylation with infertility.
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
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
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
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Volume of the periodical
19
Issue of the periodical within the volume
10
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
3877-3889
UT code for WoS article
000577157000001
EID of the result in the Scopus database
2-s2.0-85092682624