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Título: | Epitope mapping, expression and post-translational modifications of two isoforms of CD33 (CD33M and CD33m) on lymphoid and myeloid human cells. |
Fecha de publicación: | 28-ene-2011 |
Editorial: | Oxford University Press |
Cita bibliográfica: | Glycobiology, 2011, Vol. 21, Issue 6, pp. 757–770 |
ISSN: | Print: 0959-6658 Electronic: 1460-2423 |
Palabras clave: | Anti-CD33 mAb CD33 epitopes CD33m isoform |
Resumen: | We have tested the usefulness of several commercial anti-CD33 monoclonal antibodies (mAb) to determine the expression and localization of the two CD33 isoforms on several hematopoietic cell lines. The expression of the isoform CD33m, a CD33 transmembrane splice variant lacking the ligand-binding V immunoglobulin (Ig)-like domain, was detected by RT-polymerase chain reaction, western blot, confocal microscopy and flow cytometry on the membrane of several human cell types. CD33m was only detected by the anti-CD33 mAb HIM3-4 on the cell surface, whereas WM53, P67.6, 4D3, HIM3-4, WM54, D3HL60.251 or MY9 detected the CD33M isoform, indicating that HIM3-4 is the only mAb recognizing CD33 C(2) Ig domain. Accordingly, HIM3-4 binding to CD33 did not interfere with the binding of other antibodies against the CD33 V-domain. P67.6 mAb interfered with recognition by the rest of antibodies specific for the V domain. HIM3-4 staining could be increased after the sialidase treatment of all CD33(+) cells. However, this increase was stronger in activated T cells, suggesting a CD33 masking state in this cell population. Confocal microscopy analysis of CD33m HEK 293T-transfected cells revealed that this protein is expressed on the cell membrane and also detected in the Golgi compartment. CD33 is constitutively located outside the lipid raft domains, whereas cross-linked CD33 is highly recruited to this signaling platform. The unique ability of HIM3-4 mAb to detect the masking state of CD33 on different cell lineages makes it a good tool to improve the knowledge of the biological role of this sialic acid-binding Ig-like lectin. |
Autor/es principal/es: | Pérez Oliva, Ana B. Martínez Esparza, M. Vicente Fernández, José J. Corral San Miguel, Rubén García Peñarrubia, Pilar Hernández Caselles, Trinidad |
Facultad/Departamentos/Servicios: | Facultades, Departamentos, Servicios y Escuelas::Departamentos de la UMU::Bioquímica y Biología Molecular B e Inmunología |
Versión del editor: | https://academic.oup.com/glycob/article/21/6/757/1988816 |
URI: | http://hdl.handle.net/10201/142811 |
DOI: | https://doi.org/10.1093/glycob/cwq220 |
Tipo de documento: | info:eu-repo/semantics/article |
Número páginas / Extensión: | 14 |
Derechos: | info:eu-repo/semantics/embargoedAccess |
Descripción: | © The Author 2011. This document is the Published version of a Published Work that appeared in final form in Glycobiology. To access the final edited and published work see https://doi.org/10.1093/glycob/cwq220 |
Aparece en las colecciones: | Artículos: Bioquímica y Biología Molecular "B" e Inmunología |
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Fichero | Descripción | Tamaño | Formato | |
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757_002 CD33 2011.pdf | 616,92 kB | Adobe PDF | Visualizar/Abrir Solicitar una copia |
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