Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B

Autores
Giudice, J.; Barcos, L.S.; Guaimas, F.F.; Penas-Steinhardt, A.; Giordano, L.; Jares-Erijman, E.A.; Coluccio Leskow, F.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background: Insulin and insulin-like growth factors (IGFs) act on tetrameric tyrosine kinase receptors controlling essential functions including growth, metabolism, reproduction and longevity. The insulin receptor (IR) binds insulin and IGFs with different affinities triggering different cell responses. Results: We showed that IGF-II induces cell proliferation and gene transcription when IR-B is over-expressed. We combined biotinylated ligands with streptavidin conjugated quantum dots and visible fluorescent proteins to visualize the binding of IGF-II and insulin to IR-B and their ensuing internalization. By confocal microscopy and flow cytometry in living cells, we studied the internalization kinetic through the IR-B of both IGF-II, known to elicit proliferative responses, and insulin, a regulator of metabolism. Conclusions: IGF-II promotes a faster internalization of IR-B than insulin. We propose that IGF-II differentially activates mitogenic responses through endosomes, while insulin-activated IR-B remains at the plasma membrane. This fact could facilitate the interaction with key effector molecules involved in metabolism regulation. © 2013 Giudice et al.; licensee BioMed Central Ltd.
Fil:Giudice, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Giordano, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Jares-Erijman, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Coluccio Leskow, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Cell Commun. Signal. 2013;11(1)
Materia
Endocytosis
Insulin receptor
Insulin/IGF-II
Microscopy
Quantum dots
Signaling
cyan fluorescent protein
insulin
insulin receptor
insulin receptor B
quantum dot
somatomedin B
streptavidin
unclassified drug
article
biotinylation
cell membrane
cell proliferation
confocal microscopy
controlled study
endocytosis
endosome
flow cytometry
gene overexpression
genetic transcription
human
human cell
internalization
metabolic regulation
mitogenesis
priority journal
protein interaction
receptor binding
receptor upregulation
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_1478811X_v11_n1_p_Giudice
Acceder
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oai_identifier_str paperaa:paper_1478811X_v11_n1_p_Giudice
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor BGiudice, J.Barcos, L.S.Guaimas, F.F.Penas-Steinhardt, A.Giordano, L.Jares-Erijman, E.A.Coluccio Leskow, F.EndocytosisInsulin receptorInsulin/IGF-IIMicroscopyQuantum dotsSignalingcyan fluorescent proteininsulininsulin receptorinsulin receptor Bquantum dotsomatomedin Bstreptavidinunclassified drugarticlebiotinylationcell membranecell proliferationconfocal microscopycontrolled studyendocytosisendosomeflow cytometrygene overexpressiongenetic transcriptionhumanhuman cellinternalizationmetabolic regulationmitogenesispriority journalprotein interactionreceptor bindingreceptor upregulationsignal transductionBackground: Insulin and insulin-like growth factors (IGFs) act on tetrameric tyrosine kinase receptors controlling essential functions including growth, metabolism, reproduction and longevity. The insulin receptor (IR) binds insulin and IGFs with different affinities triggering different cell responses. Results: We showed that IGF-II induces cell proliferation and gene transcription when IR-B is over-expressed. We combined biotinylated ligands with streptavidin conjugated quantum dots and visible fluorescent proteins to visualize the binding of IGF-II and insulin to IR-B and their ensuing internalization. By confocal microscopy and flow cytometry in living cells, we studied the internalization kinetic through the IR-B of both IGF-II, known to elicit proliferative responses, and insulin, a regulator of metabolism. Conclusions: IGF-II promotes a faster internalization of IR-B than insulin. We propose that IGF-II differentially activates mitogenic responses through endosomes, while insulin-activated IR-B remains at the plasma membrane. This fact could facilitate the interaction with key effector molecules involved in metabolism regulation. © 2013 Giudice et al.; licensee BioMed Central Ltd.Fil:Giudice, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Giordano, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Jares-Erijman, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Coluccio Leskow, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2013info: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_1478811X_v11_n1_p_GiudiceCell Commun. Signal. 2013;11(1)reponame: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/ar2025-09-04T09:48:34Zpaperaa:paper_1478811X_v11_n1_p_GiudiceInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-04 09:48:36.245Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
title Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
spellingShingle Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
Giudice, J.
Endocytosis
Insulin receptor
Insulin/IGF-II
Microscopy
Quantum dots
Signaling
cyan fluorescent protein
insulin
insulin receptor
insulin receptor B
quantum dot
somatomedin B
streptavidin
unclassified drug
article
biotinylation
cell membrane
cell proliferation
confocal microscopy
controlled study
endocytosis
endosome
flow cytometry
gene overexpression
genetic transcription
human
human cell
internalization
metabolic regulation
mitogenesis
priority journal
protein interaction
receptor binding
receptor upregulation
signal transduction
title_short Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
title_full Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
title_fullStr Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
title_full_unstemmed Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
title_sort Insulin and insulin like growth factor II endocytosis and signaling via insulin receptor B
dc.creator.none.fl_str_mv Giudice, J.
Barcos, L.S.
Guaimas, F.F.
Penas-Steinhardt, A.
Giordano, L.
Jares-Erijman, E.A.
Coluccio Leskow, F.
author Giudice, J.
author_facet Giudice, J.
Barcos, L.S.
Guaimas, F.F.
Penas-Steinhardt, A.
Giordano, L.
Jares-Erijman, E.A.
Coluccio Leskow, F.
author_role author
author2 Barcos, L.S.
Guaimas, F.F.
Penas-Steinhardt, A.
Giordano, L.
Jares-Erijman, E.A.
Coluccio Leskow, F.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Endocytosis
Insulin receptor
Insulin/IGF-II
Microscopy
Quantum dots
Signaling
cyan fluorescent protein
insulin
insulin receptor
insulin receptor B
quantum dot
somatomedin B
streptavidin
unclassified drug
article
biotinylation
cell membrane
cell proliferation
confocal microscopy
controlled study
endocytosis
endosome
flow cytometry
gene overexpression
genetic transcription
human
human cell
internalization
metabolic regulation
mitogenesis
priority journal
protein interaction
receptor binding
receptor upregulation
signal transduction
topic Endocytosis
Insulin receptor
Insulin/IGF-II
Microscopy
Quantum dots
Signaling
cyan fluorescent protein
insulin
insulin receptor
insulin receptor B
quantum dot
somatomedin B
streptavidin
unclassified drug
article
biotinylation
cell membrane
cell proliferation
confocal microscopy
controlled study
endocytosis
endosome
flow cytometry
gene overexpression
genetic transcription
human
human cell
internalization
metabolic regulation
mitogenesis
priority journal
protein interaction
receptor binding
receptor upregulation
signal transduction
dc.description.none.fl_txt_mv Background: Insulin and insulin-like growth factors (IGFs) act on tetrameric tyrosine kinase receptors controlling essential functions including growth, metabolism, reproduction and longevity. The insulin receptor (IR) binds insulin and IGFs with different affinities triggering different cell responses. Results: We showed that IGF-II induces cell proliferation and gene transcription when IR-B is over-expressed. We combined biotinylated ligands with streptavidin conjugated quantum dots and visible fluorescent proteins to visualize the binding of IGF-II and insulin to IR-B and their ensuing internalization. By confocal microscopy and flow cytometry in living cells, we studied the internalization kinetic through the IR-B of both IGF-II, known to elicit proliferative responses, and insulin, a regulator of metabolism. Conclusions: IGF-II promotes a faster internalization of IR-B than insulin. We propose that IGF-II differentially activates mitogenic responses through endosomes, while insulin-activated IR-B remains at the plasma membrane. This fact could facilitate the interaction with key effector molecules involved in metabolism regulation. © 2013 Giudice et al.; licensee BioMed Central Ltd.
Fil:Giudice, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Giordano, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Jares-Erijman, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Coluccio Leskow, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Background: Insulin and insulin-like growth factors (IGFs) act on tetrameric tyrosine kinase receptors controlling essential functions including growth, metabolism, reproduction and longevity. The insulin receptor (IR) binds insulin and IGFs with different affinities triggering different cell responses. Results: We showed that IGF-II induces cell proliferation and gene transcription when IR-B is over-expressed. We combined biotinylated ligands with streptavidin conjugated quantum dots and visible fluorescent proteins to visualize the binding of IGF-II and insulin to IR-B and their ensuing internalization. By confocal microscopy and flow cytometry in living cells, we studied the internalization kinetic through the IR-B of both IGF-II, known to elicit proliferative responses, and insulin, a regulator of metabolism. Conclusions: IGF-II promotes a faster internalization of IR-B than insulin. We propose that IGF-II differentially activates mitogenic responses through endosomes, while insulin-activated IR-B remains at the plasma membrane. This fact could facilitate the interaction with key effector molecules involved in metabolism regulation. © 2013 Giudice et al.; licensee BioMed Central Ltd.
publishDate 2013
dc.date.none.fl_str_mv 2013
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_1478811X_v11_n1_p_Giudice
url http://hdl.handle.net/20.500.12110/paper_1478811X_v11_n1_p_Giudice
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 Cell Commun. Signal. 2013;11(1)
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
_version_ 1842340704398868480
score 12.623145

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