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Precision Glycoproteomics Reveals Distinctive N-Glycosylation in Human Spermatozoa

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F22%3A43904545" target="_blank" >RIV/60076658:12520/22:43904545 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1016/j.mcpro.2022.100214" target="_blank" >https://doi.org/10.1016/j.mcpro.2022.100214</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.mcpro.2022.100214" target="_blank" >10.1016/j.mcpro.2022.100214</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Precision Glycoproteomics Reveals Distinctive N-Glycosylation in Human Spermatozoa

  • Original language description

    Spermatozoon represents a very special cell type in human body, and glycosylation plays essential roles in its whole life including spermatogenesis, maturation, capacitation, sperm-egg recognition, and fertilization. In this study, by mapping the most comprehensive N-glycoproteome of human spermatozoa using our recently developed site-specific glycoproteomic approaches, we show that spermatozoa contain a number of distinctive glycoproteins, which are mainly involved in spermatogenesis, acrosome reaction and sperm:oocyte membrane binding, and fertilization. Heavy fucosylation is observed on 14 glycoproteins mostly located at extracellular and cell surface regions in spermatozoa but not in other tissues. Sialylation and Lewis epitopes are enriched in the biological process of immune response in spermatozoa, while bisected core structures and LacdiNAc structures are highly expressed in acrosome. These data deepen our knowledge about glycosylation in spermatozoa and lay the foundation for functional study of glycosylation and glycan structures in male 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

    30403 - Technologies involving identifying the functioning of DNA, proteins and enzymes and how they influence the onset of disease and maintenance of well-being (gene-based diagnostics and therapeutic interventions [pharmacogenomics, gene-based therapeutics])

Result continuities

  • Project

  • 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

    Molecular &amp; Cellular Proteomics

  • ISSN

    1535-9476

  • e-ISSN

  • Volume of the periodical

    21

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

    nestrankovano

  • UT code for WoS article

    000820882400001

  • EID of the result in the Scopus database

    2-s2.0-85127920679