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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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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 |
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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 |