Platelet Membrane Glycoprofiling in a PMM2-CDG Patient

Autores
Papazoglu, Gabriela Magali; Silvera Ruiz, Silene Maite; Salinas, R.; Pereira, Beatriz María Inés; Cubilla, Marisa Angelica; Pesaola, Favio Nicolas; Ghione, S.; Ramadán, N.; Martinez Duncker, I.; Asteggiano, Carla Gabriela
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Congenital disorders of glycosylation (CDG) are metabolic hereditary diseases caused by defects in the synthesis of glycoconjugates. CDG have been described in sugar-nucleotide biosynthesis and transporter, glycosyltransferases, vesicular transport, as well as in lipid biosynthesis and glycosylphosphatidylinositol anchors. PMM2-CDG is caused by mutations in the phosphomannomutase-2 (PMM2) gene and shows autosomal recessive inheritance. It affects all organs and tissues, ranging from severe psychomotor retardation to moderate intellectual disability. Alterations in the primary haemostatic system have been reported in these patients and they can lead to severe bleeding or excessive thrombosis with subsequent vascular insufficiency. Despite of being the most common CDG, platelet glycosylation and sialylation defects in PMM2-CDG patients remain incompletely characterized. In this study, we applied a lectin-based flow cytometry approach to report the first characterization of the highly glycosylated platelet membrane glycan profile in a PMM2-CDG patient. In the PMM2-CDG patient’s platelet samples, a decreased binding of SNA lectin, indicative of reduced terminal α-2-6 sialic acid content, and an increased binding of PNA lectin, suggesting desialylation of β-1-Nacetylgalactosamine residues, were observed. Reduced expression of terminal sialic acids in platelet membrane glycoproteins may contribute to the increased risk of hemorrhage reported in these patients by promoting platelet clearance and thrombocytopenia.
Fil: Papazoglu, Gabriela Magali. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Silvera Ruiz, Silene Maite. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Salinas, R.. Universidad Autónoma del Estado de Morelos; México
Fil: Pereira, Beatriz María Inés. Gobierno de la Provincia de Córdoba. Ministerio de Salud. Hospital de Niños de la Santísima Trinidad; Argentina
Fil: Cubilla, Marisa Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Pesaola, Favio Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Ghione, S.. Argenlab San Francisco; Argentina
Fil: Ramadán, N.. Fundación para el Progreso de la Medicina; Argentina
Fil: Martinez Duncker, I.. Universidad Autónoma del Estado de Morelos; México
Fil: Asteggiano, Carla Gabriela. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Materia
MASS SPECTROMETRY
PLATELET MEMBRANE
GLYCOPROFILE
PMM2-CDG
CONGENITAL DISORDERS OF GLYCOSYLATION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/152384
Acceder
id CONICETDig_3759319e1565eeb62bb886c952fa5c0f
oai_identifier_str oai:ri.conicet.gov.ar:11336/152384
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Platelet Membrane Glycoprofiling in a PMM2-CDG PatientPapazoglu, Gabriela MagaliSilvera Ruiz, Silene MaiteSalinas, R.Pereira, Beatriz María InésCubilla, Marisa AngelicaPesaola, Favio NicolasGhione, S.Ramadán, N.Martinez Duncker, I.Asteggiano, Carla GabrielaMASS SPECTROMETRYPLATELET MEMBRANEGLYCOPROFILEPMM2-CDGCONGENITAL DISORDERS OF GLYCOSYLATIONhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3https://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Congenital disorders of glycosylation (CDG) are metabolic hereditary diseases caused by defects in the synthesis of glycoconjugates. CDG have been described in sugar-nucleotide biosynthesis and transporter, glycosyltransferases, vesicular transport, as well as in lipid biosynthesis and glycosylphosphatidylinositol anchors. PMM2-CDG is caused by mutations in the phosphomannomutase-2 (PMM2) gene and shows autosomal recessive inheritance. It affects all organs and tissues, ranging from severe psychomotor retardation to moderate intellectual disability. Alterations in the primary haemostatic system have been reported in these patients and they can lead to severe bleeding or excessive thrombosis with subsequent vascular insufficiency. Despite of being the most common CDG, platelet glycosylation and sialylation defects in PMM2-CDG patients remain incompletely characterized. In this study, we applied a lectin-based flow cytometry approach to report the first characterization of the highly glycosylated platelet membrane glycan profile in a PMM2-CDG patient. In the PMM2-CDG patient’s platelet samples, a decreased binding of SNA lectin, indicative of reduced terminal α-2-6 sialic acid content, and an increased binding of PNA lectin, suggesting desialylation of β-1-Nacetylgalactosamine residues, were observed. Reduced expression of terminal sialic acids in platelet membrane glycoproteins may contribute to the increased risk of hemorrhage reported in these patients by promoting platelet clearance and thrombocytopenia.Fil: Papazoglu, Gabriela Magali. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; ArgentinaFil: Silvera Ruiz, Silene Maite. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; ArgentinaFil: Salinas, R.. Universidad Autónoma del Estado de Morelos; MéxicoFil: Pereira, Beatriz María Inés. Gobierno de la Provincia de Córdoba. Ministerio de Salud. Hospital de Niños de la Santísima Trinidad; ArgentinaFil: Cubilla, Marisa Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; ArgentinaFil: Pesaola, Favio Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; ArgentinaFil: Ghione, S.. Argenlab San Francisco; ArgentinaFil: Ramadán, N.. Fundación para el Progreso de la Medicina; ArgentinaFil: Martinez Duncker, I.. Universidad Autónoma del Estado de Morelos; MéxicoFil: Asteggiano, Carla Gabriela. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaLatin American Society Inborn Errors and Neonatal Screening2021-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/152384Papazoglu, Gabriela Magali; Silvera Ruiz, Silene Maite; Salinas, R.; Pereira, Beatriz María Inés; Cubilla, Marisa Angelica; et al.; Platelet Membrane Glycoprofiling in a PMM2-CDG Patient; Latin American Society Inborn Errors and Neonatal Screening; Journal of Inborn Errors of Metabolism and Screening; 9; 8-2021; 1-112326-4594CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.scielo.br/j/jiems/a/Wwp5rLqqSLrB3GkB39qMHjB/?lang=eninfo:eu-repo/semantics/altIdentifier/doi/10.1590/2326-4594-jiems-2020-0030info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:43:37Zoai:ri.conicet.gov.ar:11336/152384instacron: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:34982025-09-29 10:43:37.286CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
title Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
spellingShingle Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
Papazoglu, Gabriela Magali
MASS SPECTROMETRY
PLATELET MEMBRANE
GLYCOPROFILE
PMM2-CDG
CONGENITAL DISORDERS OF GLYCOSYLATION
title_short Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
title_full Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
title_fullStr Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
title_full_unstemmed Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
title_sort Platelet Membrane Glycoprofiling in a PMM2-CDG Patient
dc.creator.none.fl_str_mv Papazoglu, Gabriela Magali
Silvera Ruiz, Silene Maite
Salinas, R.
Pereira, Beatriz María Inés
Cubilla, Marisa Angelica
Pesaola, Favio Nicolas
Ghione, S.
Ramadán, N.
Martinez Duncker, I.
Asteggiano, Carla Gabriela
author Papazoglu, Gabriela Magali
author_facet Papazoglu, Gabriela Magali
Silvera Ruiz, Silene Maite
Salinas, R.
Pereira, Beatriz María Inés
Cubilla, Marisa Angelica
Pesaola, Favio Nicolas
Ghione, S.
Ramadán, N.
Martinez Duncker, I.
Asteggiano, Carla Gabriela
author_role author
author2 Silvera Ruiz, Silene Maite
Salinas, R.
Pereira, Beatriz María Inés
Cubilla, Marisa Angelica
Pesaola, Favio Nicolas
Ghione, S.
Ramadán, N.
Martinez Duncker, I.
Asteggiano, Carla Gabriela
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv MASS SPECTROMETRY
PLATELET MEMBRANE
GLYCOPROFILE
PMM2-CDG
CONGENITAL DISORDERS OF GLYCOSYLATION
topic MASS SPECTROMETRY
PLATELET MEMBRANE
GLYCOPROFILE
PMM2-CDG
CONGENITAL DISORDERS OF GLYCOSYLATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.1
https://purl.org/becyt/ford/3
https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Congenital disorders of glycosylation (CDG) are metabolic hereditary diseases caused by defects in the synthesis of glycoconjugates. CDG have been described in sugar-nucleotide biosynthesis and transporter, glycosyltransferases, vesicular transport, as well as in lipid biosynthesis and glycosylphosphatidylinositol anchors. PMM2-CDG is caused by mutations in the phosphomannomutase-2 (PMM2) gene and shows autosomal recessive inheritance. It affects all organs and tissues, ranging from severe psychomotor retardation to moderate intellectual disability. Alterations in the primary haemostatic system have been reported in these patients and they can lead to severe bleeding or excessive thrombosis with subsequent vascular insufficiency. Despite of being the most common CDG, platelet glycosylation and sialylation defects in PMM2-CDG patients remain incompletely characterized. In this study, we applied a lectin-based flow cytometry approach to report the first characterization of the highly glycosylated platelet membrane glycan profile in a PMM2-CDG patient. In the PMM2-CDG patient’s platelet samples, a decreased binding of SNA lectin, indicative of reduced terminal α-2-6 sialic acid content, and an increased binding of PNA lectin, suggesting desialylation of β-1-Nacetylgalactosamine residues, were observed. Reduced expression of terminal sialic acids in platelet membrane glycoproteins may contribute to the increased risk of hemorrhage reported in these patients by promoting platelet clearance and thrombocytopenia.
Fil: Papazoglu, Gabriela Magali. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Silvera Ruiz, Silene Maite. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Salinas, R.. Universidad Autónoma del Estado de Morelos; México
Fil: Pereira, Beatriz María Inés. Gobierno de la Provincia de Córdoba. Ministerio de Salud. Hospital de Niños de la Santísima Trinidad; Argentina
Fil: Cubilla, Marisa Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Pesaola, Favio Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina
Fil: Ghione, S.. Argenlab San Francisco; Argentina
Fil: Ramadán, N.. Fundación para el Progreso de la Medicina; Argentina
Fil: Martinez Duncker, I.. Universidad Autónoma del Estado de Morelos; México
Fil: Asteggiano, Carla Gabriela. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Estudio de las Metabolopatías Congénitas. Cátedra de Clínica Pediátrica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
description Congenital disorders of glycosylation (CDG) are metabolic hereditary diseases caused by defects in the synthesis of glycoconjugates. CDG have been described in sugar-nucleotide biosynthesis and transporter, glycosyltransferases, vesicular transport, as well as in lipid biosynthesis and glycosylphosphatidylinositol anchors. PMM2-CDG is caused by mutations in the phosphomannomutase-2 (PMM2) gene and shows autosomal recessive inheritance. It affects all organs and tissues, ranging from severe psychomotor retardation to moderate intellectual disability. Alterations in the primary haemostatic system have been reported in these patients and they can lead to severe bleeding or excessive thrombosis with subsequent vascular insufficiency. Despite of being the most common CDG, platelet glycosylation and sialylation defects in PMM2-CDG patients remain incompletely characterized. In this study, we applied a lectin-based flow cytometry approach to report the first characterization of the highly glycosylated platelet membrane glycan profile in a PMM2-CDG patient. In the PMM2-CDG patient’s platelet samples, a decreased binding of SNA lectin, indicative of reduced terminal α-2-6 sialic acid content, and an increased binding of PNA lectin, suggesting desialylation of β-1-Nacetylgalactosamine residues, were observed. Reduced expression of terminal sialic acids in platelet membrane glycoproteins may contribute to the increased risk of hemorrhage reported in these patients by promoting platelet clearance and thrombocytopenia.
publishDate 2021
dc.date.none.fl_str_mv 2021-08
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/11336/152384
Papazoglu, Gabriela Magali; Silvera Ruiz, Silene Maite; Salinas, R.; Pereira, Beatriz María Inés; Cubilla, Marisa Angelica; et al.; Platelet Membrane Glycoprofiling in a PMM2-CDG Patient; Latin American Society Inborn Errors and Neonatal Screening; Journal of Inborn Errors of Metabolism and Screening; 9; 8-2021; 1-11
2326-4594
CONICET Digital
CONICET
url http://hdl.handle.net/11336/152384
identifier_str_mv Papazoglu, Gabriela Magali; Silvera Ruiz, Silene Maite; Salinas, R.; Pereira, Beatriz María Inés; Cubilla, Marisa Angelica; et al.; Platelet Membrane Glycoprofiling in a PMM2-CDG Patient; Latin American Society Inborn Errors and Neonatal Screening; Journal of Inborn Errors of Metabolism and Screening; 9; 8-2021; 1-11
2326-4594
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.scielo.br/j/jiems/a/Wwp5rLqqSLrB3GkB39qMHjB/?lang=en
info:eu-repo/semantics/altIdentifier/doi/10.1590/2326-4594-jiems-2020-0030
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Latin American Society Inborn Errors and Neonatal Screening
publisher.none.fl_str_mv Latin American Society Inborn Errors and Neonatal Screening
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
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score 13.070432

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