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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/14012
Ver los metadatos del registro completo
id |
CONICETDig_399228129d04019d8bff7788503e2015 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/14012 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
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 |
_version_ |
1842268869171871744 |
score |
13.13397 |