Please use this identifier to cite or link to this item: http://hdl.handle.net/10201/74885

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dc.contributor.authorElola, María T.-
dc.contributor.authorFerragut, Fátima-
dc.contributor.authorCárdenas Delgado, Víctor M.-
dc.contributor.authorNugnes, Lorena G.-
dc.contributor.authorGentilini, Lucas-
dc.contributor.authorLaderach, Diego-
dc.contributor.authorTroncoso, María F.-
dc.contributor.authorCompagno, Daniel-
dc.contributor.authorWolfenstein-Tode, Carlota-
dc.contributor.authorRabinovich, Gabriel A.-
dc.date.accessioned2019-09-25T14:28:45Z-
dc.date.available2019-09-25T14:28:45Z-
dc.date.issued2014-
dc.identifier.citationHistology and Histopathology, vol. 29, nº 9, (2014)es_ES
dc.identifier.issn1699-5848-
dc.identifier.issn0213-3911-
dc.identifier.urihttp://hdl.handle.net/10201/74885-
dc.description.abstractGalectin-8 (Gal-8) is a ‘tandem-repeat’-type galectin, which possesses two carbohydrate recognition domains connected by a linker peptide. Gal-8 complexity is related to the alternative splicing of its mRNA precursor, which is known to generate isoforms. Regarding its carbohydrate-binding specificity, Gal-8 has a unique feature among galectins, since its Cterminal domain has higher affinity for N-glycan-type branched oligosaccharides, while its N-terminal domain shows strong affinity for α2-3-sialylated or 3’-sulfated ß-galactosides. We integrate here the available information on Gal-8 expression in different tumor types and attempt to elucidate associations of its expression and localization during tumor progression with the overarching goal of analyzing its potential applications in diagnosis and prognosis. Differential diagnosis is still a prime concern in tumor pathology, and Gal-8 could be of great value in some types of primary or secondary tumors (i.e. papillary thyroid carcinoma, advanced colon carcinoma from patients with distant metastases, or metastases from primary lung carcinoma). The prognostic value of Gal-8 has been described for laryngeal carcinoma as well as advanced colon carcinoma. Further studies are needed to explain the relevance of Gal-8 and its isoforms in tumor pathology and their different intra- or extracellular roles (cytoplasmic, nuclear or extracellular) in tumor biology.es_ES
dc.formatapplication/pdfes_ES
dc.format.extent13es_ES
dc.languageenges_ES
dc.publisherF. Hernández y Juan F. Madrid. Universidad de Murcia: Departamento de Biología Celular e Histologíaes_ES
dc.rightsinfo:eu-repo/semantics/openAccess*
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectGalectin-8es_ES
dc.subjectIsoformses_ES
dc.subjectTumorses_ES
dc.subjectLunges_ES
dc.subject.otherCDU::5 - Ciencias puras y naturales::57 - Biología::576 - Biología celular y subcelular. Citologíaes_ES
dc.titleExpression, localization and function of galectin-8, a tandem-repeat lectin, in human tumorses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
Appears in Collections:Vol.29, nº 9 (2014)

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