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https://doi.org/10.1186/1750-1172-8-170


Título: | GPI-anchor and GPI-anchored protein expression in PMM2-CDG patients |
Fecha de publicación: | 2013 |
Cita bibliográfica: | Orphanet Journal of Rare Diseases 2013, 8:170. |
ISSN: | Electronic: 1750-1172 |
Palabras clave: | PMM2-CDG N-glycosylation defects GPI-anchor and GPI-anchored proteins |
Resumen: | Background: Mutations in PMM2 impair phosphomannomutase-2 activity and cause the most frequent congenital disorder of glycosylation, PMM2-CDG. Mannose-1-phosphate, that is deficient in this disorder, is also implicated in the biosynthesis of glycosylphosphatidyl inositol (GPI) anchors. Objective: To evaluate whether GPI-anchor and GPI-anchored proteins are defective in PMM2-CDG patients. Methods: The expression of GPI-anchor and seven GPI-anchored proteins was evaluated by flow cytometry in different cell types from twelve PMM2-CDG patients. Additionally, neutrophil CD16 and plasma hepatic proteins were studied by Western blot. Transferrin glycoforms were evaluated by HPLC. Results: Patients and controls had similar surface expression of GPI-anchor and most GPI-anchored proteins. Nevertheless, patients displayed a significantly diminished binding of two anti-CD16 antibodies (3G8 and KD1) to neutrophils and also of anti-CD14 (61D3) to monocytes. Interestingly, CD16 immunostaining and asialotransferrin levels significantly correlated with patients' age. Analysis by flow cytometry of CD14 with MΦP9, and CD16 expression in neutrophils by Western blot using H-80 ruled out deficiencies of these antigens. Conclusions: PMM2 mutations do not impair GPI-anchor or GPI-anchored protein expression. However, the glycosylation anomalies caused by PMM2 mutations might affect the immunoreactivity of monoclonal antibodies and lead to incorrect conclusions about the expression of different proteins, including GPI-anchored proteins. Neutrophils and monocytes are sensitive to PMM2 mutations, leading to abnormal glycosylation in immune receptors, which might potentially affect their affinity to their ligands, and contribute to infection. This study also confirms less severe hypoglycosylation defects in older PMM2-CDG patients. |
Autor/es principal/es: | Morena-Barrio, María Eugenia de la Hernández-Caselles, Trinidad Corral, Javier García-López, Roberto Martínez-Martínez, Irene Pérez-Dueñas, Belén Altisent, Carmen Sevivas, Teresa Kristensen, Soren Guillén-Navarro, Encarna Miñano, Antonia Vicente, Vicente Jaeken, Jaak Lozano, María Luisa |
Facultad/Departamentos/Servicios: | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Medicina |
URI: | http://hdl.handle.net/10201/138891 |
DOI: | https://doi.org/10.1186/1750-1172-8-170 |
Tipo de documento: | info:eu-repo/semantics/article |
Número páginas / Extensión: | 10 |
Derechos: | info:eu-repo/semantics/openAccess Attribution-NonCommercial-NoDerivatives 4.0 Internacional |
Descripción: | © 2013 de la Morena-Barrio et al.; licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited |
Aparece en las colecciones: | Artículos: Medicina |
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