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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2014
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paper:paper_02133911_v29_n9_p1093_Elola2023-06-08T15:20:48Z Expression, localization and function of galectin-8, a tandem-repeat lectin, in human tumors 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. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02133911_v29_n9_p1093_Elola 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 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. |
| 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 |
| publishDate |
2014 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02133911_v29_n9_p1093_Elola http://hdl.handle.net/20.500.12110/paper_02133911_v29_n9_p1093_Elola |
| _version_ |
1768543032106287104 |