Cargando…

Siglec Ligands

A dense and diverse array of glycans on glycoproteins and glycolipids decorate all cell surfaces. In vertebrates, many of these carry sialic acid, in a variety of linkages and glycan contexts, as their outermost sugar moiety. Among their functions, glycans engage complementary glycan binding protein...

Descripción completa

Detalles Bibliográficos
Autores principales: Gonzalez-Gil, Anabel, Schnaar, Ronald L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8161119/
https://www.ncbi.nlm.nih.gov/pubmed/34065256
http://dx.doi.org/10.3390/cells10051260
_version_ 1783700436633518080
author Gonzalez-Gil, Anabel
Schnaar, Ronald L.
author_facet Gonzalez-Gil, Anabel
Schnaar, Ronald L.
author_sort Gonzalez-Gil, Anabel
collection PubMed
description A dense and diverse array of glycans on glycoproteins and glycolipids decorate all cell surfaces. In vertebrates, many of these carry sialic acid, in a variety of linkages and glycan contexts, as their outermost sugar moiety. Among their functions, glycans engage complementary glycan binding proteins (lectins) to regulate cell physiology. Among the glycan binding proteins are the Siglecs, sialic acid binding immunoglobulin-like lectins. In humans, there are 14 Siglecs, most of which are expressed on overlapping subsets of immune system cells. Each Siglec engages distinct, endogenous sialylated glycans that initiate signaling programs and regulate cellular responses. Here, we explore the emerging science of Siglec ligands, including endogenous sialoglycoproteins and glycolipids and synthetic sialomimetics. Knowledge in this field promises to reveal new molecular pathways controlling cell physiology and new opportunities for therapeutic intervention.
format Online
Article
Text
id pubmed-8161119
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-81611192021-05-29 Siglec Ligands Gonzalez-Gil, Anabel Schnaar, Ronald L. Cells Review A dense and diverse array of glycans on glycoproteins and glycolipids decorate all cell surfaces. In vertebrates, many of these carry sialic acid, in a variety of linkages and glycan contexts, as their outermost sugar moiety. Among their functions, glycans engage complementary glycan binding proteins (lectins) to regulate cell physiology. Among the glycan binding proteins are the Siglecs, sialic acid binding immunoglobulin-like lectins. In humans, there are 14 Siglecs, most of which are expressed on overlapping subsets of immune system cells. Each Siglec engages distinct, endogenous sialylated glycans that initiate signaling programs and regulate cellular responses. Here, we explore the emerging science of Siglec ligands, including endogenous sialoglycoproteins and glycolipids and synthetic sialomimetics. Knowledge in this field promises to reveal new molecular pathways controlling cell physiology and new opportunities for therapeutic intervention. MDPI 2021-05-20 /pmc/articles/PMC8161119/ /pubmed/34065256 http://dx.doi.org/10.3390/cells10051260 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Gonzalez-Gil, Anabel
Schnaar, Ronald L.
Siglec Ligands
title Siglec Ligands
title_full Siglec Ligands
title_fullStr Siglec Ligands
title_full_unstemmed Siglec Ligands
title_short Siglec Ligands
title_sort siglec ligands
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8161119/
https://www.ncbi.nlm.nih.gov/pubmed/34065256
http://dx.doi.org/10.3390/cells10051260
work_keys_str_mv AT gonzalezgilanabel siglecligands
AT schnaarronaldl siglecligands