Functions of cell surface galectin-glycoprotein lattices

Autores
Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis.
Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Toscano, Marta Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Jackson, Shawn S.. University of Maryland; Estados Unidos
Fil: Vasta, Gerardo R.. University of Maryland; Estados Unidos
Materia
GALECTINS
B-LYMPHOCYTES
INMUNITY
CELL MEMBRANE
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:11336/26257
Acceder
id CONICETDig_bf6736b573460ba5d3636c496be512c3
oai_identifier_str oai:ri.conicet.gov.ar:11336/26257
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Functions of cell surface galectin-glycoprotein latticesRabinovich, Gabriel AdriánToscano, Marta AliciaJackson, Shawn S.Vasta, Gerardo R.GALECTINSB-LYMPHOCYTESINMUNITYCELL MEMBRANEhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3https://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis.Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Toscano, Marta Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Jackson, Shawn S.. University of Maryland; Estados UnidosFil: Vasta, Gerardo R.. University of Maryland; Estados UnidosElsevier2007-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/26257Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.; Functions of cell surface galectin-glycoprotein lattices; Elsevier; Current Opinion In Structural Biology; 17; 5; 10-2007; 513-5200959-440X1879-033XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0959440X07001303info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2007.09.002info:eu-repo/semantics/altIdentifier/pmid/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2100406/info:eu-repo/semantics/altIdentifier/pmid/17950594info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:29:41Zoai:ri.conicet.gov.ar:11336/26257instacron: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:34982025-10-22 11:29:41.944CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Functions of cell surface galectin-glycoprotein lattices
title Functions of cell surface galectin-glycoprotein lattices
spellingShingle Functions of cell surface galectin-glycoprotein lattices
Rabinovich, Gabriel Adrián
GALECTINS
B-LYMPHOCYTES
INMUNITY
CELL MEMBRANE
title_short Functions of cell surface galectin-glycoprotein lattices
title_full Functions of cell surface galectin-glycoprotein lattices
title_fullStr Functions of cell surface galectin-glycoprotein lattices
title_full_unstemmed Functions of cell surface galectin-glycoprotein lattices
title_sort Functions of cell surface galectin-glycoprotein lattices
dc.creator.none.fl_str_mv Rabinovich, Gabriel Adrián
Toscano, Marta Alicia
Jackson, Shawn S.
Vasta, Gerardo R.
author Rabinovich, Gabriel Adrián
author_facet Rabinovich, Gabriel Adrián
Toscano, Marta Alicia
Jackson, Shawn S.
Vasta, Gerardo R.
author_role author
author2 Toscano, Marta Alicia
Jackson, Shawn S.
Vasta, Gerardo R.
author2_role author
author
author
dc.subject.none.fl_str_mv GALECTINS
B-LYMPHOCYTES
INMUNITY
CELL MEMBRANE
topic GALECTINS
B-LYMPHOCYTES
INMUNITY
CELL MEMBRANE
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis.
Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Toscano, Marta Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Jackson, Shawn S.. University of Maryland; Estados Unidos
Fil: Vasta, Gerardo R.. University of Maryland; Estados Unidos
description Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis.
publishDate 2007
dc.date.none.fl_str_mv 2007-10
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/11336/26257
Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.; Functions of cell surface galectin-glycoprotein lattices; Elsevier; Current Opinion In Structural Biology; 17; 5; 10-2007; 513-520
0959-440X
1879-033X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/26257
identifier_str_mv Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.; Functions of cell surface galectin-glycoprotein lattices; Elsevier; Current Opinion In Structural Biology; 17; 5; 10-2007; 513-520
0959-440X
1879-033X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0959440X07001303
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2007.09.002
info:eu-repo/semantics/altIdentifier/pmid/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2100406/
info:eu-repo/semantics/altIdentifier/pmid/17950594
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
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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_ 1846781884437102592
score 12.982451

Publicaciones similares