Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview

Autores
Salatino, Mariana; Rabinovich, Gabriel Adrian
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In recent years, we have witnessed critical advances in genomics and proteomics which contributed to delineate the "tumor progression signature". This includes the altered expression of genes and proteins not only in tumor cells, but also in tumor-associated stromal, endothelial, and immune cells. Adding more complexity to this bewildering information, efforts are being made to define the "glycosylation signature" of the tumor microenvironment, which results from the abnormal expression and activity of glycosyltransferases, glycosidases, and enzyme chaperons. The multiple combinatorial possibilities of glycan structures expressed by neoplastic versus normal tissue provide enormous potential for information display and expand potential therapeutic opportunities. The responsibility of deciphering the biological information encoded by the tumor-associated glycome is partially assigned, to distinct families of endogenous glycan-binding proteins or lectins, whose expression and function are regulated in cancerous tissues. Galectins, a family of evolutionarily conserved glycan-binding proteins, can control tumor progression by directly influencing tumor growth or by modulating cell migration, angiogenesis, and tumor-immune escape. In this review, we will highlight recent findings on how galectin-glycan lattices control the dialogue between tumor and immune cells and how these interactions could be exploited for therapeutic purposes.
Fil: Salatino, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Rabinovich, Gabriel Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Materia
Tumor
Immune Response
Glycans
Lectins
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/14012

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spelling Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overviewSalatino, MarianaRabinovich, Gabriel AdrianTumorImmune ResponseGlycansLectinshttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3In recent years, we have witnessed critical advances in genomics and proteomics which contributed to delineate the "tumor progression signature". This includes the altered expression of genes and proteins not only in tumor cells, but also in tumor-associated stromal, endothelial, and immune cells. Adding more complexity to this bewildering information, efforts are being made to define the "glycosylation signature" of the tumor microenvironment, which results from the abnormal expression and activity of glycosyltransferases, glycosidases, and enzyme chaperons. The multiple combinatorial possibilities of glycan structures expressed by neoplastic versus normal tissue provide enormous potential for information display and expand potential therapeutic opportunities. The responsibility of deciphering the biological information encoded by the tumor-associated glycome is partially assigned, to distinct families of endogenous glycan-binding proteins or lectins, whose expression and function are regulated in cancerous tissues. Galectins, a family of evolutionarily conserved glycan-binding proteins, can control tumor progression by directly influencing tumor growth or by modulating cell migration, angiogenesis, and tumor-immune escape. In this review, we will highlight recent findings on how galectin-glycan lattices control the dialogue between tumor and immune cells and how these interactions could be exploited for therapeutic purposes.Fil: Salatino, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); ArgentinaFil: Rabinovich, Gabriel Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaHumana Press2011-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/14012Salatino, Mariana; Rabinovich, Gabriel Adrian; Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview; Humana Press; Methods In Molecular Biology (clifton, N.j.); 677; 2-2011; 355-3741064-37451940-6029enginfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/protocol/10.1007%2F978-1-60761-869-0_23info:eu-repo/semantics/altIdentifier/doi/10.1007/978-1-60761-869-0_23info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:47:35Zoai:ri.conicet.gov.ar:11336/14012instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:47:35.833CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
title Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
spellingShingle Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
Salatino, Mariana
Tumor
Immune Response
Glycans
Lectins
title_short Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
title_full Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
title_fullStr Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
title_full_unstemmed Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
title_sort Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview
dc.creator.none.fl_str_mv Salatino, Mariana
Rabinovich, Gabriel Adrian
author Salatino, Mariana
author_facet Salatino, Mariana
Rabinovich, Gabriel Adrian
author_role author
author2 Rabinovich, Gabriel Adrian
author2_role author
dc.subject.none.fl_str_mv Tumor
Immune Response
Glycans
Lectins
topic Tumor
Immune Response
Glycans
Lectins
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv In recent years, we have witnessed critical advances in genomics and proteomics which contributed to delineate the "tumor progression signature". This includes the altered expression of genes and proteins not only in tumor cells, but also in tumor-associated stromal, endothelial, and immune cells. Adding more complexity to this bewildering information, efforts are being made to define the "glycosylation signature" of the tumor microenvironment, which results from the abnormal expression and activity of glycosyltransferases, glycosidases, and enzyme chaperons. The multiple combinatorial possibilities of glycan structures expressed by neoplastic versus normal tissue provide enormous potential for information display and expand potential therapeutic opportunities. The responsibility of deciphering the biological information encoded by the tumor-associated glycome is partially assigned, to distinct families of endogenous glycan-binding proteins or lectins, whose expression and function are regulated in cancerous tissues. Galectins, a family of evolutionarily conserved glycan-binding proteins, can control tumor progression by directly influencing tumor growth or by modulating cell migration, angiogenesis, and tumor-immune escape. In this review, we will highlight recent findings on how galectin-glycan lattices control the dialogue between tumor and immune cells and how these interactions could be exploited for therapeutic purposes.
Fil: Salatino, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Fil: Rabinovich, Gabriel Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
description In recent years, we have witnessed critical advances in genomics and proteomics which contributed to delineate the "tumor progression signature". This includes the altered expression of genes and proteins not only in tumor cells, but also in tumor-associated stromal, endothelial, and immune cells. Adding more complexity to this bewildering information, efforts are being made to define the "glycosylation signature" of the tumor microenvironment, which results from the abnormal expression and activity of glycosyltransferases, glycosidases, and enzyme chaperons. The multiple combinatorial possibilities of glycan structures expressed by neoplastic versus normal tissue provide enormous potential for information display and expand potential therapeutic opportunities. The responsibility of deciphering the biological information encoded by the tumor-associated glycome is partially assigned, to distinct families of endogenous glycan-binding proteins or lectins, whose expression and function are regulated in cancerous tissues. Galectins, a family of evolutionarily conserved glycan-binding proteins, can control tumor progression by directly influencing tumor growth or by modulating cell migration, angiogenesis, and tumor-immune escape. In this review, we will highlight recent findings on how galectin-glycan lattices control the dialogue between tumor and immune cells and how these interactions could be exploited for therapeutic purposes.
publishDate 2011
dc.date.none.fl_str_mv 2011-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/14012
Salatino, Mariana; Rabinovich, Gabriel Adrian; Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview; Humana Press; Methods In Molecular Biology (clifton, N.j.); 677; 2-2011; 355-374
1064-3745
1940-6029
url http://hdl.handle.net/11336/14012
identifier_str_mv Salatino, Mariana; Rabinovich, Gabriel Adrian; Fine-tuning antitumor responses through the control of galectin-glycan interactions: an overview; Humana Press; Methods In Molecular Biology (clifton, N.j.); 677; 2-2011; 355-374
1064-3745
1940-6029
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/protocol/10.1007%2F978-1-60761-869-0_23
info:eu-repo/semantics/altIdentifier/doi/10.1007/978-1-60761-869-0_23
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Humana Press
publisher.none.fl_str_mv Humana Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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