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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • 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

  • 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