Galectin-1: Biphasic growth regulation of Leydig tumor cells
Galectin-1 (Gal-1) is a widely expressed β-galactoside-binding protein that exerts pleiotropic biological functions. To gain insight into the potential role of Gal-1 as a novel modulator of Leydig cells, we investigated its effect on the growth and death of MA-10 tumor Leydig cells. In this study, w...
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paper:paper_09596658_v16_n9_p810_Biron2023-06-08T15:57:02Z Galectin-1: Biphasic growth regulation of Leydig tumor cells Troncoso, María Fernanda Patrignani, Zoraida Judith Pignataro, Omar Pedro Apoptosis Galectin-1 Leydig cells Proliferation caspase 3 caspase 8 caspase 8 inhibitor caspase 9 caspase 9 inhibitor cytochrome c death receptor disaccharide DNA fragment FAS ligand galectin 1 lactose animal cell apoptosis article carbohydrate analysis cell growth cell membrane potential cell proliferation controlled study cytofluorometry enzyme activation growth regulation Leydig cell Leydig cell tumor male mitochondrial membrane mouse nonhuman pathophysiology priority journal protein determination protein expression protein function protein secretion Cell Line, Tumor Cell Proliferation Cytoplasm DNA Fragmentation Dose-Response Relationship, Drug Galectin 1 Gene Expression Regulation, Neoplastic Humans Lactose Leydig Cells Male Membrane Potentials Mitochondria Neoplasm Proteins Sertoli-Leydig Cell Tumor Testicular Neoplasms Galectin-1 (Gal-1) is a widely expressed β-galactoside-binding protein that exerts pleiotropic biological functions. To gain insight into the potential role of Gal-1 as a novel modulator of Leydig cells, we investigated its effect on the growth and death of MA-10 tumor Leydig cells. In this study, we identified cytoplasmic Gal-1 expression in these tumor cells by cytofluorometry. DNA fragmentation, caspase-3, -8, and -9 activation, loss of mitochondrial membrane potential (ΔΨ m), cytochrome c (Cyt c) release, and FasL expression suggested that relatively high concentrations of exogenously added recombinant Gal-1 (rGal-1) induced apoptosis by the mitochondrial and death receptor pathways. These pathways were independently activated, as the presence of the inhibitor of caspase-8 or -9 only partially prevented Gal-1-effect. On the contrary, low concentrations of Gal-1 significantly promoted cell proliferation, without inducing cell death. Importantly, the presence of the disaccharide lactose prevented Gal-1 effects, suggesting the involvement of the carbohydrate recognition domain (CRD). This study provides strong evidence that Gal-1 is a novel biphasic regulator of Leydig tumor cell number, suggesting a novel role for Gal-1 in the reproductive physiopathology. © Copyright 2006 Oxford University Press. Fil:Troncoso, M.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Patrignani, Z.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pignataro, O.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2006 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09596658_v16_n9_p810_Biron http://hdl.handle.net/20.500.12110/paper_09596658_v16_n9_p810_Biron |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Apoptosis Galectin-1 Leydig cells Proliferation caspase 3 caspase 8 caspase 8 inhibitor caspase 9 caspase 9 inhibitor cytochrome c death receptor disaccharide DNA fragment FAS ligand galectin 1 lactose animal cell apoptosis article carbohydrate analysis cell growth cell membrane potential cell proliferation controlled study cytofluorometry enzyme activation growth regulation Leydig cell Leydig cell tumor male mitochondrial membrane mouse nonhuman pathophysiology priority journal protein determination protein expression protein function protein secretion Cell Line, Tumor Cell Proliferation Cytoplasm DNA Fragmentation Dose-Response Relationship, Drug Galectin 1 Gene Expression Regulation, Neoplastic Humans Lactose Leydig Cells Male Membrane Potentials Mitochondria Neoplasm Proteins Sertoli-Leydig Cell Tumor Testicular Neoplasms |
spellingShingle |
Apoptosis Galectin-1 Leydig cells Proliferation caspase 3 caspase 8 caspase 8 inhibitor caspase 9 caspase 9 inhibitor cytochrome c death receptor disaccharide DNA fragment FAS ligand galectin 1 lactose animal cell apoptosis article carbohydrate analysis cell growth cell membrane potential cell proliferation controlled study cytofluorometry enzyme activation growth regulation Leydig cell Leydig cell tumor male mitochondrial membrane mouse nonhuman pathophysiology priority journal protein determination protein expression protein function protein secretion Cell Line, Tumor Cell Proliferation Cytoplasm DNA Fragmentation Dose-Response Relationship, Drug Galectin 1 Gene Expression Regulation, Neoplastic Humans Lactose Leydig Cells Male Membrane Potentials Mitochondria Neoplasm Proteins Sertoli-Leydig Cell Tumor Testicular Neoplasms Troncoso, María Fernanda Patrignani, Zoraida Judith Pignataro, Omar Pedro Galectin-1: Biphasic growth regulation of Leydig tumor cells |
topic_facet |
Apoptosis Galectin-1 Leydig cells Proliferation caspase 3 caspase 8 caspase 8 inhibitor caspase 9 caspase 9 inhibitor cytochrome c death receptor disaccharide DNA fragment FAS ligand galectin 1 lactose animal cell apoptosis article carbohydrate analysis cell growth cell membrane potential cell proliferation controlled study cytofluorometry enzyme activation growth regulation Leydig cell Leydig cell tumor male mitochondrial membrane mouse nonhuman pathophysiology priority journal protein determination protein expression protein function protein secretion Cell Line, Tumor Cell Proliferation Cytoplasm DNA Fragmentation Dose-Response Relationship, Drug Galectin 1 Gene Expression Regulation, Neoplastic Humans Lactose Leydig Cells Male Membrane Potentials Mitochondria Neoplasm Proteins Sertoli-Leydig Cell Tumor Testicular Neoplasms |
description |
Galectin-1 (Gal-1) is a widely expressed β-galactoside-binding protein that exerts pleiotropic biological functions. To gain insight into the potential role of Gal-1 as a novel modulator of Leydig cells, we investigated its effect on the growth and death of MA-10 tumor Leydig cells. In this study, we identified cytoplasmic Gal-1 expression in these tumor cells by cytofluorometry. DNA fragmentation, caspase-3, -8, and -9 activation, loss of mitochondrial membrane potential (ΔΨ m), cytochrome c (Cyt c) release, and FasL expression suggested that relatively high concentrations of exogenously added recombinant Gal-1 (rGal-1) induced apoptosis by the mitochondrial and death receptor pathways. These pathways were independently activated, as the presence of the inhibitor of caspase-8 or -9 only partially prevented Gal-1-effect. On the contrary, low concentrations of Gal-1 significantly promoted cell proliferation, without inducing cell death. Importantly, the presence of the disaccharide lactose prevented Gal-1 effects, suggesting the involvement of the carbohydrate recognition domain (CRD). This study provides strong evidence that Gal-1 is a novel biphasic regulator of Leydig tumor cell number, suggesting a novel role for Gal-1 in the reproductive physiopathology. © Copyright 2006 Oxford University Press. |
author |
Troncoso, María Fernanda Patrignani, Zoraida Judith Pignataro, Omar Pedro |
author_facet |
Troncoso, María Fernanda Patrignani, Zoraida Judith Pignataro, Omar Pedro |
author_sort |
Troncoso, María Fernanda |
title |
Galectin-1: Biphasic growth regulation of Leydig tumor cells |
title_short |
Galectin-1: Biphasic growth regulation of Leydig tumor cells |
title_full |
Galectin-1: Biphasic growth regulation of Leydig tumor cells |
title_fullStr |
Galectin-1: Biphasic growth regulation of Leydig tumor cells |
title_full_unstemmed |
Galectin-1: Biphasic growth regulation of Leydig tumor cells |
title_sort |
galectin-1: biphasic growth regulation of leydig tumor cells |
publishDate |
2006 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09596658_v16_n9_p810_Biron http://hdl.handle.net/20.500.12110/paper_09596658_v16_n9_p810_Biron |
work_keys_str_mv |
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1768544603983577088 |