Endogenous lectins shape the function of dendritic cells and tailor adaptive immunity: Mechanisms and biomedical applications
In spite of their central role in orchestrating immunity, dendritic cells (DCs) can also limit harmful reactions and promote immune tolerance by inducing T cell anergy or favoring the differentiation of T regulatory (Treg) cells. Several factors may influence the ‘decision’ of DCs to become immunoge...
| Autores: | , , , , , |
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| Tipo de documento: | artigo |
| Estado: | Versão publicada |
| Data de publicação: | 2011 |
| País: | Argentina |
| Recursos: | Consejo Nacional de Investigaciones Científicas y Técnicas |
| Repositório: | CONICET Digital (CONICET) |
| Idioma: | inglês |
| OAI Identifier: | oai:ri.conicet.gov.ar:11336/11670 |
| Acesso em linha: | http://hdl.handle.net/11336/11670 |
| Access Level: | Acceso aberto |
| Palavra-chave: | Lectins Galectins C-Type Lectins Siglecs Dendritic Cells https://purl.org/becyt/ford/3.1 https://purl.org/becyt/ford/3 |
| Resumo: | In spite of their central role in orchestrating immunity, dendritic cells (DCs) can also limit harmful reactions and promote immune tolerance by inducing T cell anergy or favoring the differentiation of T regulatory (Treg) cells. Several factors may influence the ‘decision’ of DCs to become immunogenic or tolerogenic including the nature of antigenic challenge, the engagement of selective pathogen recognition receptors (PRRs) and the balance of cytokines and growth factors. In addition, mounting evidence indicates a key role of endogenous lectins including C-type lectins, siglecs and galectins in shaping DC immunogenicity and tailoring adaptive immune responses, through recognition of specific ‘glycan signatures’ on invading pathogens or host cells. While galectins are in general secreted proteins that act in a paracrine or autocrine manner, all known siglecs and most C-type lectins are membrane-bound receptors that convey glycan-containing information into DC differentiation or maturation programs. Yet, some of the signaling pathways triggered by endogenous lectins converge in similar functional outcomes regardless of divergences in their structure, homology or glycanbinding specificity. To gain a more complete understanding on the role of protein–glycan interactions in DC biology, here we will integrate scattered information on these structurally-divergent but functionally-related lectins and their potential biomedical applications. |
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