Gangliosides as Siglec ligands.
CD33
Macrophages
Myelin-associated glycoprotein
Natural killer cells
Sialic acid
Sialoadhesin
Journal
Glycoconjugate journal
ISSN: 1573-4986
Titre abrégé: Glycoconj J
Pays: United States
ID NLM: 8603310
Informations de publication
Date de publication:
04 2023
04 2023
Historique:
received:
29
11
2022
accepted:
13
01
2023
revised:
09
01
2023
pubmed:
27
1
2023
medline:
23
3
2023
entrez:
26
1
2023
Statut:
ppublish
Résumé
The structure of a sialoglycan can be translated into to a biological response when it binds to a specific endogenous lectin. Among endogenous sialic acid-binding lectins in humans are those comprising the 15-member Siglec family, most of which are expressed on overlapping sets of immune cells. Endogenous Siglec ligands are sialoglycolipids (gangliosides) and/or sialoglycoproteins, on cell surfaces or in the extracellular milieu, that bind to and initiate signaling by cell surface Siglecs. In the nervous system, where gangliosides are the predominant sialoglycans, Siglec-4 (myelin-associated glycoprotein) on myelinating cells binds to gangliosides GD1a and GT1b on nerve cell axons to ensure stable and productive axon-myelin interactions. In the immune system, Siglec-7 on natural killer cells binds to gangliosides GD3 and GD2 to inhibit immune signaling. Expression of GD3 and GD2 on cancer cells can lead to tumor immune evasion. Siglec-1 (sialoadhesin, CD169) on macrophages binds to gangliosides on tumors and enveloped viruses. This may enhance antigen presentation in some cases, or increase viral distribution in others. Several other Siglecs bind to gangliosides in vitro, the biological significance of which has yet to be fully established. Gangliosides, which are found on all human cells and tissues in cell-specific distributions, are functional Siglec ligands with varied roles driving Siglec-mediated signaling.
Identifiants
pubmed: 36701102
doi: 10.1007/s10719-023-10101-2
pii: 10.1007/s10719-023-10101-2
doi:
Substances chimiques
Sialic Acid Binding Immunoglobulin-like Lectins
0
Ligands
0
Gangliosides
0
Types de publication
Journal Article
Review
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
159-167Subventions
Organisme : NCI NIH HHS
ID : U01 CA241953
Pays : United States
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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