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Oligosaccharide Ligands of Galectin-4 and Its Subunits: Multivalency Scores Highly

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F23%3A00573084" target="_blank" >RIV/61388971:_____/23:00573084 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/23:10472928 RIV/60461373:22330/23:43927265

  • Result on the web

    <a href="https://www.mdpi.com/1420-3049/28/10/4039" target="_blank" >https://www.mdpi.com/1420-3049/28/10/4039</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/molecules28104039" target="_blank" >10.3390/molecules28104039</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Oligosaccharide Ligands of Galectin-4 and Its Subunits: Multivalency Scores Highly

  • Original language description

    Galectins are carbohydrate-binding lectins that modulate the proliferation, apoptosis, adhesion, or migration of cells by cross-linking glycans on cell membranes or extracellular matrix components. Galectin-4 (Gal-4) is a tandem-repeat-type galectin expressed mainly in the epithelial cells of the gastrointestinal tract. It consists of an N- and a C-terminal carbohydrate-binding domain (CRD), each with distinct binding affinities, interconnected with a peptide linker. Compared to other more abundant galectins, the knowledge of the pathophysiology of Gal-4 is sparse. Its altered expression in tumor tissue is associated with, for example, colon, colorectal, and liver cancers, and it increases in tumor progression, and metastasis. There is also very limited information on the preferences of Gal-4 for its carbohydrate ligands, particularly with respect to Gal-4 subunits. Similarly, there is virtually no information on the interaction of Gal-4 with multivalent ligands. This work shows the expression and purification of Gal-4 and its subunits and presents a structure-affinity relationship study with a library of oligosaccharide ligands. Furthermore, the influence of multivalency is demonstrated in the interaction with a model lactosyl-decorated synthetic glycoconjugate. The present data may be used in biomedical research for the design of efficient ligands of Gal-4 with diagnostic or therapeutic potential.

  • 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/GF22-00197K" target="_blank" >GF22-00197K: Chemo-enzymatic synthesis of selective multivalent neo-glycoproteins for galectin-4 inhibition</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Molecules

  • ISSN

    1420-3049

  • e-ISSN

    1420-3049

  • Volume of the periodical

    28

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    15

  • Pages from-to

    4039

  • UT code for WoS article

    000998092900001

  • EID of the result in the Scopus database

    2-s2.0-85160591247