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dc.contributor.author
Ruggiero, Fernando Miguel
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dc.contributor.author
Vilcaes, Aldo Alejandro
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dc.contributor.author
Yuki, Nobuhiro
dc.contributor.author
Daniotti, Jose Luis
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dc.date.available
2018-11-16T14:48:51Z
dc.date.issued
2017-01
dc.identifier.citation
Ruggiero, Fernando Miguel; Vilcaes, Aldo Alejandro; Yuki, Nobuhiro; Daniotti, Jose Luis; Membrane binding, endocytic trafficking and intracellular fate of high-affinity antibodies to gangliosides GD1a and GM1; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1859; 1; 1-2017; 80-93
dc.identifier.issn
0005-2736
dc.identifier.uri
http://hdl.handle.net/11336/64585
dc.description.abstract
Gangliosides are glycolipids embedded in the outer leaflets of the plasma membrane. Antibodies against GM1 and GD1a gangliosides are associated with selective dysfunction of motor axons in peripheral neuropathies, and differential endocytic processing of antibodies to gangliosides represent a critical modulator of site-specific injury in Guillain-Barré syndrome. In addition, antibodies to glycolipids have emerged as an attractive tool for therapeutic interventions in cancer. In this work, we have investigated the binding, endocytosis and intracellular fate of high-affinity antibodies to gangliosides GD1a and GM1 both in epithelial and neuronal-like cells. Live cell imaging and fluorometric analysis showed that, after specific plasma membrane binding, a fraction of antibody to GD1a was slightly but rapidly internalized by a dynamin 2-independent pathway and then accumulated in the endocytic recycling compartment. We also show that internalization of antibody to GD1a is regulated by ADP-ribosylation factor 6. Surprisingly, experiment of cellular antibody uptake performed at 16 °C, widely used to accumulate the endocytic cargo in sorting endosomes, showed that the antibody to GD1a remained mostly localized at the plasma membrane, supporting the presence of selective mechanisms for cell internalization of antibody-ganglioside complex. In contrast, antibody to GM1 was endocyted in epithelial cells but remained at the plasma membrane of neuronal-like cells. Together, these results provide additional evidences about the molecular mechanisms that operate in the uptake and intracellular trafficking dynamics of antibodies to glycolipids and have significant translational implications for the understanding of clinical characteristics of anti-ganglioside antibody-mediated neuropathies and for the development of novel therapeutics targeting.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Anti-Ganglioside Antibody
dc.subject
Autoimmune Neuropathy
dc.subject
Endocytosis
dc.subject
Ganglioside
dc.subject
Intracellular Trafficking
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Membrane binding, endocytic trafficking and intracellular fate of high-affinity antibodies to gangliosides GD1a and GM1
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-10-22T16:48:18Z
dc.journal.volume
1859
dc.journal.number
1
dc.journal.pagination
80-93
dc.journal.pais
Países Bajos
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dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Ruggiero, Fernando Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil
Fil: Vilcaes, Aldo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil
Fil: Yuki, Nobuhiro. Department Of Neurology, Mishima Hospital; Japón
dc.description.fil
Fil: Daniotti, Jose Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.journal.title
Biochimica et Biophysica Acta - Biomembranes
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/j.bbamem.2016.10.020
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273616303534?via%3Dihub
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