Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings

Autores
Laderach, D.J.; Compagno, D.; Toscano, M.A.; Croci, D.O.; Dergan-Dylon, S.; Salatino, M.; Rabinovich, G.A.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Galectins are a family of evolutionarily conserved animal lectins with pleiotropic functions and widespread distribution. Fifteen members have been identified in a wide variety of cells and tissues. Through recognition of cell surface glycoproteins and glycolipids, these endogenous lectins can trigger a cascade of intracellular signaling pathways capable of modulating cell differentiation, proliferation, survival, and migration. These cellular events are critical in a variety of biological processes including embryogenesis, angiogenesis, neurogenesis, and immunity and are substantially altered during tumorigenesis, neurodegeneration, and inflammation. In addition, galectins can modulate intracellular functions and this effect involves direct interactions with distinct signaling pathways. In this review, we discuss current knowledge on the intracellular signaling pathways triggered by this multifunctional family of β-galactoside-binding proteins in selected physiological and pathological settings. Understanding the "galectin signalosome" will be essential to delineate rational therapeutic strategies based on the specific control of galectin expression and function. © 2009 IUBMB.
Fil:Toscano, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Croci, D.O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Salatino, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
IUBMB Life 2010;62(1):1-13
Materia
Apoptosis
Differentiation
Galectins
Immune regulation
Oncogenesis
Signaling pathways
galaptin
galectin
glycan
galectin
polysaccharide
cell adhesion
cell differentiation
cell proliferation
cell transformation
connective tissue
embryo development
hematopoietic system
nervous tissue
protein expression
protein function
protein interaction
review
signal transduction
tumor cell
animal
hematopoiesis
human
metabolism
neoplasm
pathophysiology
physiology
signal transduction
Animalia
Animals
Galectins
Hematopoiesis
Humans
Neoplasms
Polysaccharides
Signal Transduction
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_15216543_v62_n1_p1_Laderach

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network_name_str Biblioteca Digital (UBA-FCEN)
spelling Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settingsLaderach, D.J.Compagno, D.Toscano, M.A.Croci, D.O.Dergan-Dylon, S.Salatino, M.Rabinovich, G.A.ApoptosisDifferentiationGalectinsImmune regulationOncogenesisSignaling pathwaysgalaptingalectinglycangalectinpolysaccharidecell adhesioncell differentiationcell proliferationcell transformationconnective tissueembryo developmenthematopoietic systemnervous tissueprotein expressionprotein functionprotein interactionreviewsignal transductiontumor cellanimalhematopoiesishumanmetabolismneoplasmpathophysiologyphysiologysignal transductionAnimaliaAnimalsGalectinsHematopoiesisHumansNeoplasmsPolysaccharidesSignal TransductionGalectins are a family of evolutionarily conserved animal lectins with pleiotropic functions and widespread distribution. Fifteen members have been identified in a wide variety of cells and tissues. Through recognition of cell surface glycoproteins and glycolipids, these endogenous lectins can trigger a cascade of intracellular signaling pathways capable of modulating cell differentiation, proliferation, survival, and migration. These cellular events are critical in a variety of biological processes including embryogenesis, angiogenesis, neurogenesis, and immunity and are substantially altered during tumorigenesis, neurodegeneration, and inflammation. In addition, galectins can modulate intracellular functions and this effect involves direct interactions with distinct signaling pathways. In this review, we discuss current knowledge on the intracellular signaling pathways triggered by this multifunctional family of β-galactoside-binding proteins in selected physiological and pathological settings. Understanding the "galectin signalosome" will be essential to delineate rational therapeutic strategies based on the specific control of galectin expression and function. © 2009 IUBMB.Fil:Toscano, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Croci, D.O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Salatino, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2010info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_15216543_v62_n1_p1_LaderachIUBMB Life 2010;62(1):1-13reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-10-23T11:18:18Zpaperaa:paper_15216543_v62_n1_p1_LaderachInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-23 11:18:20.073Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
title Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
spellingShingle Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
Laderach, D.J.
Apoptosis
Differentiation
Galectins
Immune regulation
Oncogenesis
Signaling pathways
galaptin
galectin
glycan
galectin
polysaccharide
cell adhesion
cell differentiation
cell proliferation
cell transformation
connective tissue
embryo development
hematopoietic system
nervous tissue
protein expression
protein function
protein interaction
review
signal transduction
tumor cell
animal
hematopoiesis
human
metabolism
neoplasm
pathophysiology
physiology
signal transduction
Animalia
Animals
Galectins
Hematopoiesis
Humans
Neoplasms
Polysaccharides
Signal Transduction
title_short Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
title_full Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
title_fullStr Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
title_full_unstemmed Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
title_sort Dissecting the signal transduction pathways triggered by galectin-glycan interactions in physiological and pathological settings
dc.creator.none.fl_str_mv Laderach, D.J.
Compagno, D.
Toscano, M.A.
Croci, D.O.
Dergan-Dylon, S.
Salatino, M.
Rabinovich, G.A.
author Laderach, D.J.
author_facet Laderach, D.J.
Compagno, D.
Toscano, M.A.
Croci, D.O.
Dergan-Dylon, S.
Salatino, M.
Rabinovich, G.A.
author_role author
author2 Compagno, D.
Toscano, M.A.
Croci, D.O.
Dergan-Dylon, S.
Salatino, M.
Rabinovich, G.A.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Apoptosis
Differentiation
Galectins
Immune regulation
Oncogenesis
Signaling pathways
galaptin
galectin
glycan
galectin
polysaccharide
cell adhesion
cell differentiation
cell proliferation
cell transformation
connective tissue
embryo development
hematopoietic system
nervous tissue
protein expression
protein function
protein interaction
review
signal transduction
tumor cell
animal
hematopoiesis
human
metabolism
neoplasm
pathophysiology
physiology
signal transduction
Animalia
Animals
Galectins
Hematopoiesis
Humans
Neoplasms
Polysaccharides
Signal Transduction
topic Apoptosis
Differentiation
Galectins
Immune regulation
Oncogenesis
Signaling pathways
galaptin
galectin
glycan
galectin
polysaccharide
cell adhesion
cell differentiation
cell proliferation
cell transformation
connective tissue
embryo development
hematopoietic system
nervous tissue
protein expression
protein function
protein interaction
review
signal transduction
tumor cell
animal
hematopoiesis
human
metabolism
neoplasm
pathophysiology
physiology
signal transduction
Animalia
Animals
Galectins
Hematopoiesis
Humans
Neoplasms
Polysaccharides
Signal Transduction
dc.description.none.fl_txt_mv Galectins are a family of evolutionarily conserved animal lectins with pleiotropic functions and widespread distribution. Fifteen members have been identified in a wide variety of cells and tissues. Through recognition of cell surface glycoproteins and glycolipids, these endogenous lectins can trigger a cascade of intracellular signaling pathways capable of modulating cell differentiation, proliferation, survival, and migration. These cellular events are critical in a variety of biological processes including embryogenesis, angiogenesis, neurogenesis, and immunity and are substantially altered during tumorigenesis, neurodegeneration, and inflammation. In addition, galectins can modulate intracellular functions and this effect involves direct interactions with distinct signaling pathways. In this review, we discuss current knowledge on the intracellular signaling pathways triggered by this multifunctional family of β-galactoside-binding proteins in selected physiological and pathological settings. Understanding the "galectin signalosome" will be essential to delineate rational therapeutic strategies based on the specific control of galectin expression and function. © 2009 IUBMB.
Fil:Toscano, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Croci, D.O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Salatino, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Galectins are a family of evolutionarily conserved animal lectins with pleiotropic functions and widespread distribution. Fifteen members have been identified in a wide variety of cells and tissues. Through recognition of cell surface glycoproteins and glycolipids, these endogenous lectins can trigger a cascade of intracellular signaling pathways capable of modulating cell differentiation, proliferation, survival, and migration. These cellular events are critical in a variety of biological processes including embryogenesis, angiogenesis, neurogenesis, and immunity and are substantially altered during tumorigenesis, neurodegeneration, and inflammation. In addition, galectins can modulate intracellular functions and this effect involves direct interactions with distinct signaling pathways. In this review, we discuss current knowledge on the intracellular signaling pathways triggered by this multifunctional family of β-galactoside-binding proteins in selected physiological and pathological settings. Understanding the "galectin signalosome" will be essential to delineate rational therapeutic strategies based on the specific control of galectin expression and function. © 2009 IUBMB.
publishDate 2010
dc.date.none.fl_str_mv 2010
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/20.500.12110/paper_15216543_v62_n1_p1_Laderach
url http://hdl.handle.net/20.500.12110/paper_15216543_v62_n1_p1_Laderach
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv IUBMB Life 2010;62(1):1-13
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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