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Complexity and modification of the bull sperm glycocalyx during epididymal maturation

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F24%3A00586446" target="_blank" >RIV/86652036:_____/24:00586446 - isvavai.cz</a>

  • Alternative codes found

    RIV/60460709:41210/24:98491

  • Result on the web

    <a href="https://faseb.onlinelibrary.wiley.com/doi/epdf/10.1096/fj.202400551RR" target="_blank" >https://faseb.onlinelibrary.wiley.com/doi/epdf/10.1096/fj.202400551RR</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1096/fj.202400551RR" target="_blank" >10.1096/fj.202400551RR</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Complexity and modification of the bull sperm glycocalyx during epididymal maturation

  • Original language description

    Mammalian spermatozoa have a surface covered with glycocalyx, consisting of heterogeneous glycoproteins and glycolipids. This complexity arises from diverse monosaccharides, distinct linkages, various isomeric glycans, branching levels, and saccharide sequences. The glycocalyx is synthesized by spermatozoa developing in the testis, and its subsequent alterations during their transit through the epididymis are a critical process for the sperm acquisition of fertilizing ability. In this study, we performed detailed analysis of the glycocalyx on the sperm surface of bull spermatozoa in relation to individual parts of the epididymis using a wide range (24) of lectins with specific carbohydrate binding preferences. Fluorescence analysis of intact sperm isolated from the bull epididymides was complemented by Western blot detection of protein extracts from the sperm plasma membrane fractions. Our experimental results revealed predominant sequential modification of bull sperm glycans with N-acetyllactosamine (LacNAc), followed by subsequent sialylation and fucosylation in a highly specific manner. Additionally, variations in the lectin detection on the sperm surface may indicate the acquisition or release of glycans or glycoproteins. Our study is the first to provide a complex analysis of the bull sperm glycocalyx modification during epididymal maturation.

  • 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

    <a href="/en/project/GA22-31156S" target="_blank" >GA22-31156S: Key molecules involved in gamete maturation and sperm-zona pellucida recognition in pig and cattle</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2024

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    FASEB Journal

  • ISSN

    0892-6638

  • e-ISSN

    1530-6860

  • Volume of the periodical

    38

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    23

  • Pages from-to

    e23687

  • UT code for WoS article

    001230210500001

  • EID of the result in the Scopus database

    2-s2.0-85194127693