Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors

Galectin-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...

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Autor principal: Elola, M.T
Otros Autores: Ferragut, F., Cárdenas Delgado, V.M, Nugnes, L.G, Gentilini, L., Laderach, D., Troncoso, M.F, Compagno, D., Wolfenstein-Todel, C., Rabinovich, G.A
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Histology and Histopathology 2014
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-84905663943 
024 7 |2 cas  |a Galectins; LGALS8 protein, human; Tumor Markers, Biological 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a HIHIE 
100 1 |a Elola, M.T. 
245 1 0 |a Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors 
260 |b Histology and Histopathology  |c 2014 
270 1 0 |m Elola, M. T.; Universidad de Buenos Aires, Junín 956 (C1113), Buenos Aires, Argentina; email: mt_elola@yahoo.com 
506 |2 openaire  |e Política editorial 
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520 3 |a Galectin-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 C-terminal 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.  |l eng 
593 |a Institute of Biochemistry and Biophysics (IQUIFIB), UBA-CONICET, Department of Biological Chemistry, School of Pharmacy and Biochemistry. University of Buenos Aires, Argentina 
593 |a Laboratory of Functional Glycomics, IQUIBICEN, CONICET, Department of Biological Chemistry, School of Exact and Natural Sciences, University of Buenos Aires, Argentina 
593 |a Laboratory of Immunopathology, Institute of Experimental Biology and Medicine (IBYME), NICET, Buenos Aires, Argentina 
690 1 0 |a GALECTIN-8 
690 1 0 |a ISOFORMS 
690 1 0 |a LUNG 
690 1 0 |a PROSTATE 
690 1 0 |a TUMORS 
690 1 0 |a GALECTIN 
690 1 0 |a LGALS8 PROTEIN, HUMAN 
690 1 0 |a TUMOR MARKER 
690 1 0 |a HUMAN 
690 1 0 |a METABOLISM 
690 1 0 |a NEOPLASM 
690 1 0 |a PATHOLOGY 
690 1 0 |a GALECTINS 
690 1 0 |a HUMANS 
690 1 0 |a NEOPLASMS 
690 1 0 |a TUMOR MARKERS, BIOLOGICAL 
700 1 |a Ferragut, F. 
700 1 |a Cárdenas Delgado, V.M. 
700 1 |a Nugnes, L.G. 
700 1 |a Gentilini, L. 
700 1 |a Laderach, D. 
700 1 |a Troncoso, M.F. 
700 1 |a Compagno, D. 
700 1 |a Wolfenstein-Todel, C. 
700 1 |a Rabinovich, G.A. 
773 0 |d Histology and Histopathology, 2014  |g v. 29  |h pp. 1093-1105  |k n. 9  |p Histol. Histopathol.  |x 02133911  |t Histology and Histopathology 
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