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dc.creatorZabalegui, N. (Natalia)-
dc.creatorLopez-Diaz-de-Cerio, A. (Ascensión)-
dc.creatorInoges, S. (Susana)-
dc.creatorRodriguez-Calvillo, M. (Mercedes)-
dc.creatorPerez-Calvo, J. (Javier)-
dc.creatorHernandez, M. (Milagros)-
dc.creatorGarcia-Foncillas, J. (Jesús)-
dc.creatorMartin-Algarra, S. (Salvador)-
dc.creatorRocha, E. (Eduardo)-
dc.creatorBendandi, M. (Maurizio)-
dc.date.accessioned2024-02-08T12:33:38Z-
dc.date.available2024-02-08T12:33:38Z-
dc.date.issued2004-
dc.identifier.citationZabalegui, N. (Natalia); Lopez-Diaz-de-Cerio, A. (Ascensión); Inoges, S. (Susana); et al. "Acquired potential N-glycosylation sites within the tumor-specific immunoglobulin heavy chains of B-cell malignancies". Haematologica. 89, 2004, 541 - 546es
dc.identifier.issn0390-6078-
dc.identifier.urihttps://hdl.handle.net/10171/68922-
dc.description.abstractBackground and Objectives. Among B-cell malignancies, follicular lymphomas (FL) more frequently show acquired, potential N-glycosylation sites (AGS) within tumor-specific immunoglobulin. The aim of this study was to extend this observation and to evaluate the pattern of presentation of AGS within five different forms of B-cell lymphoma. Design and Methods. We sequenced the tumor-specific immunoglobulin heavy chain variable region fragment, including complementarity-determining regions 2 and 3, of forty-seven consecutive patients with a B-cell malignancy enrolled in idiotype vaccine clinical trials. This sequencing approach is known to allow the identification of most AGS. We then statistically analyzed differences in presentation pattern, in terms of tumor histology, immunoglobulin isotype, AGS location and amino acid composition. Results. All twenty-four FL cases presented with at least one AGS, whereas the vast majority of four B-cell lymphoma types other than FL did not. The non- FL group of tumors included four cases of Burkitt’s lymphoma, six of diffuse large cell lymphoma, seven man- tle cell lymphomas and six small lymphocytic lymphomas. Most IgM-bearing follicular lymphoma cases featured their AGS within complementarity-determining region 2, as opposed to those bearing an IgG, which mostly displayed the AGS within complementar- ity-determining region 3. The vast majority of AGS located within either complementarity-determining region ended with a serine residue, whereas those located within frame- work regions mostly featured threonine as the last amino acid residue. Interpretation and Conclusions. In our series, all cases of FL had AGS within their tumor-specific immunoglobulin heavy chain variable regions. In contrast, most B-cell malignancies other than FL did not. Further studies are warranted in order to establish the possible meaning of these findings in terms of disease pathogenesis, their diagnostic value in doubtful cases and their potential implications for immunotherapy.es_ES
dc.language.isoenges_ES
dc.publisherFerrata Storti Foundationes_ES
dc.rightsinfo:eu-repo/semantics/closedAccesses_ES
dc.subjectGlycosylation siteses_ES
dc.subjectImmunoglobulines_ES
dc.subjectB-cell malignancieses_ES
dc.subjectIsotypees_ES
dc.titleAcquired potential N-glycosylation sites within the tumor-specific immunoglobulin heavy chains of B-cell malignancieses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dadun.citation.endingPage546es_ES
dadun.citation.publicationNameHaematologicaes_ES
dadun.citation.startingPage541es_ES
dadun.citation.volume89es_ES

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