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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Autores principales: Elola, M.T., Ferragut, F., Cárdenas Delgado, V.M., Nugnes, L.G., Gentilini, L., Laderach, D., Troncoso, M.F., Compagno, D., Wolfenstein-Todel, C., Rabinovich, G.A.
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_02133911_v29_n9_p1093_Elola
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spelling todo:paper_02133911_v29_n9_p1093_Elola2023-10-03T15:10:07Z Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors Elola, M.T. Ferragut, F. Cárdenas Delgado, V.M. Nugnes, L.G. Gentilini, L. Laderach, D. Troncoso, M.F. Compagno, D. Wolfenstein-Todel, C. Rabinovich, G.A. Galectin-8 Isoforms Lung Prostate Tumors galectin LGALS8 protein, human tumor marker human metabolism neoplasm pathology Galectins Humans Neoplasms Tumor Markers, Biological 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_02133911_v29_n9_p1093_Elola
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Galectin-8
Isoforms
Lung
Prostate
Tumors
galectin
LGALS8 protein, human
tumor marker
human
metabolism
neoplasm
pathology
Galectins
Humans
Neoplasms
Tumor Markers, Biological
spellingShingle Galectin-8
Isoforms
Lung
Prostate
Tumors
galectin
LGALS8 protein, human
tumor marker
human
metabolism
neoplasm
pathology
Galectins
Humans
Neoplasms
Tumor Markers, Biological
Elola, M.T.
Ferragut, F.
Cárdenas Delgado, V.M.
Nugnes, L.G.
Gentilini, L.
Laderach, D.
Troncoso, M.F.
Compagno, D.
Wolfenstein-Todel, C.
Rabinovich, G.A.
Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors
topic_facet Galectin-8
Isoforms
Lung
Prostate
Tumors
galectin
LGALS8 protein, human
tumor marker
human
metabolism
neoplasm
pathology
Galectins
Humans
Neoplasms
Tumor Markers, Biological
description 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.
format JOUR
author Elola, M.T.
Ferragut, F.
Cárdenas Delgado, V.M.
Nugnes, L.G.
Gentilini, L.
Laderach, D.
Troncoso, M.F.
Compagno, D.
Wolfenstein-Todel, C.
Rabinovich, G.A.
author_facet Elola, M.T.
Ferragut, F.
Cárdenas Delgado, V.M.
Nugnes, L.G.
Gentilini, L.
Laderach, D.
Troncoso, M.F.
Compagno, D.
Wolfenstein-Todel, C.
Rabinovich, G.A.
author_sort Elola, M.T.
title Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors
title_short Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors
title_full Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors
title_fullStr Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors
title_full_unstemmed Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors
title_sort expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors
url http://hdl.handle.net/20.500.12110/paper_02133911_v29_n9_p1093_Elola
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