AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs

Autores
Mercer, Natalia; Ahmed, Hafiz; McCarthy, Antonio Desmond; Etcheverry, Susana B.; Vasta, Gerardo R.; Cortizo, Ana María
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión enviada
Descripción
The accumulation of irreversible advanced glycation endproducts (AGEs) on long-lived proteins, and the interaction of AGEs with cellular receptors such as AGE-R3/galectin-3 and RAGE, are considered to be key events in the development of longterm complications of diabetes mellitus, Alzheimer’s disease, uremia and ageing. The aim of this study was to investigate the expression and sub-cellular distribution of galectin-3, as well as its possible modulation by AGEs, in MC3T3E1 mouse calvaria-derived osteoblasts and in UMR 106 rat osteosarcoma cells. Both osteoblastic lines were cultured either with control bovine serum albumin (BSA) or with AGEs-BSA for 48 h. Cells were evaluated for galectin-3 expression by fixing and immunofluorescent microscopic analysis; or Western blot analysis of whole cell extracts, sub-cellular fractions and culture media. Both cell lines express 30 kDa (monomeric) galectin-3, although expression was about 15-fold lower in the UMR106 osteosarcoma cells. Dimeric (70 kDa) galectin-3 was additionally observed in the UMR106 cells. Immunofluorescent analysis of galectin-3 distribution showed a diffuse cytoplasmic and strong nuclear pattern in MC3T3E1 osteoblasts, and a patchy cytoplasmic pattern in UMR106 cells. Western blot analysis for both cell lines showed that galectin-3 was mainly found in the cytoplasm and in minor amounts in the microsomal fraction, while considerable amounts were secreted into the culture media. Exposure to 100–200 μg/mL AGEs-BSA increased the cellular content of 30 kDa galectin-3 (20–25% for MC3T3E1 and 35–70% for UMR106 versus control BSA, p < 0.05), and decreased the culture media levels of galectin-3 (10–20% for MC3T3E1 and for UMR106 versus control BSA, p < 0.05). These results confirm the expression of galectin-3 in osteoblastic cells, and suggest different levels and sub-cellular distribution of this protein in transformed versus non-transformed osteoblasts. Osteoblastic exposure to AGEs alters their expression and secretion of galectin-3, which could have significant consequences on osteoblast metabolism and thus on bone turnover.
Materia
Ciencias Químicas
galectin-3
advanced glycation endproducts
osteoblasts
bone
regulation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
CIC Digital (CICBA)
Institución
Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
OAI Identificador
oai:digital.cic.gba.gob.ar:11746/4949

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network_acronym_str CICBA
repository_id_str 9441
network_name_str CIC Digital (CICBA)
spelling AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEsMercer, NataliaAhmed, HafizMcCarthy, Antonio DesmondEtcheverry, Susana B.Vasta, Gerardo R.Cortizo, Ana MaríaCiencias Químicasgalectin-3advanced glycation endproductsosteoblastsboneregulationThe accumulation of irreversible advanced glycation endproducts (AGEs) on long-lived proteins, and the interaction of AGEs with cellular receptors such as AGE-R3/galectin-3 and RAGE, are considered to be key events in the development of longterm complications of diabetes mellitus, Alzheimer’s disease, uremia and ageing. The aim of this study was to investigate the expression and sub-cellular distribution of galectin-3, as well as its possible modulation by AGEs, in MC3T3E1 mouse calvaria-derived osteoblasts and in UMR 106 rat osteosarcoma cells. Both osteoblastic lines were cultured either with control bovine serum albumin (BSA) or with AGEs-BSA for 48 h. Cells were evaluated for galectin-3 expression by fixing and immunofluorescent microscopic analysis; or Western blot analysis of whole cell extracts, sub-cellular fractions and culture media. Both cell lines express 30 kDa (monomeric) galectin-3, although expression was about 15-fold lower in the UMR106 osteosarcoma cells. Dimeric (70 kDa) galectin-3 was additionally observed in the UMR106 cells. Immunofluorescent analysis of galectin-3 distribution showed a diffuse cytoplasmic and strong nuclear pattern in MC3T3E1 osteoblasts, and a patchy cytoplasmic pattern in UMR106 cells. Western blot analysis for both cell lines showed that galectin-3 was mainly found in the cytoplasm and in minor amounts in the microsomal fraction, while considerable amounts were secreted into the culture media. Exposure to 100–200 μg/mL AGEs-BSA increased the cellular content of 30 kDa galectin-3 (20–25% for MC3T3E1 and 35–70% for UMR106 versus control BSA, p < 0.05), and decreased the culture media levels of galectin-3 (10–20% for MC3T3E1 and for UMR106 versus control BSA, p < 0.05). These results confirm the expression of galectin-3 in osteoblastic cells, and suggest different levels and sub-cellular distribution of this protein in transformed versus non-transformed osteoblasts. Osteoblastic exposure to AGEs alters their expression and secretion of galectin-3, which could have significant consequences on osteoblast metabolism and thus on bone turnover.2004info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://digital.cic.gba.gob.ar/handle/11746/4949enginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/reponame:CIC Digital (CICBA)instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Airesinstacron:CICBA2025-09-29T13:39:53Zoai:digital.cic.gba.gob.ar:11746/4949Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-09-29 13:39:53.298CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse
dc.title.none.fl_str_mv AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
title AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
spellingShingle AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
Mercer, Natalia
Ciencias Químicas
galectin-3
advanced glycation endproducts
osteoblasts
bone
regulation
title_short AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
title_full AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
title_fullStr AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
title_full_unstemmed AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
title_sort AGE-R3/galectin-3 expression in osteoblast-like cells: Regulation by AGEs
dc.creator.none.fl_str_mv Mercer, Natalia
Ahmed, Hafiz
McCarthy, Antonio Desmond
Etcheverry, Susana B.
Vasta, Gerardo R.
Cortizo, Ana María
author Mercer, Natalia
author_facet Mercer, Natalia
Ahmed, Hafiz
McCarthy, Antonio Desmond
Etcheverry, Susana B.
Vasta, Gerardo R.
Cortizo, Ana María
author_role author
author2 Ahmed, Hafiz
McCarthy, Antonio Desmond
Etcheverry, Susana B.
Vasta, Gerardo R.
Cortizo, Ana María
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Químicas
galectin-3
advanced glycation endproducts
osteoblasts
bone
regulation
topic Ciencias Químicas
galectin-3
advanced glycation endproducts
osteoblasts
bone
regulation
dc.description.none.fl_txt_mv The accumulation of irreversible advanced glycation endproducts (AGEs) on long-lived proteins, and the interaction of AGEs with cellular receptors such as AGE-R3/galectin-3 and RAGE, are considered to be key events in the development of longterm complications of diabetes mellitus, Alzheimer’s disease, uremia and ageing. The aim of this study was to investigate the expression and sub-cellular distribution of galectin-3, as well as its possible modulation by AGEs, in MC3T3E1 mouse calvaria-derived osteoblasts and in UMR 106 rat osteosarcoma cells. Both osteoblastic lines were cultured either with control bovine serum albumin (BSA) or with AGEs-BSA for 48 h. Cells were evaluated for galectin-3 expression by fixing and immunofluorescent microscopic analysis; or Western blot analysis of whole cell extracts, sub-cellular fractions and culture media. Both cell lines express 30 kDa (monomeric) galectin-3, although expression was about 15-fold lower in the UMR106 osteosarcoma cells. Dimeric (70 kDa) galectin-3 was additionally observed in the UMR106 cells. Immunofluorescent analysis of galectin-3 distribution showed a diffuse cytoplasmic and strong nuclear pattern in MC3T3E1 osteoblasts, and a patchy cytoplasmic pattern in UMR106 cells. Western blot analysis for both cell lines showed that galectin-3 was mainly found in the cytoplasm and in minor amounts in the microsomal fraction, while considerable amounts were secreted into the culture media. Exposure to 100–200 μg/mL AGEs-BSA increased the cellular content of 30 kDa galectin-3 (20–25% for MC3T3E1 and 35–70% for UMR106 versus control BSA, p < 0.05), and decreased the culture media levels of galectin-3 (10–20% for MC3T3E1 and for UMR106 versus control BSA, p < 0.05). These results confirm the expression of galectin-3 in osteoblastic cells, and suggest different levels and sub-cellular distribution of this protein in transformed versus non-transformed osteoblasts. Osteoblastic exposure to AGEs alters their expression and secretion of galectin-3, which could have significant consequences on osteoblast metabolism and thus on bone turnover.
description The accumulation of irreversible advanced glycation endproducts (AGEs) on long-lived proteins, and the interaction of AGEs with cellular receptors such as AGE-R3/galectin-3 and RAGE, are considered to be key events in the development of longterm complications of diabetes mellitus, Alzheimer’s disease, uremia and ageing. The aim of this study was to investigate the expression and sub-cellular distribution of galectin-3, as well as its possible modulation by AGEs, in MC3T3E1 mouse calvaria-derived osteoblasts and in UMR 106 rat osteosarcoma cells. Both osteoblastic lines were cultured either with control bovine serum albumin (BSA) or with AGEs-BSA for 48 h. Cells were evaluated for galectin-3 expression by fixing and immunofluorescent microscopic analysis; or Western blot analysis of whole cell extracts, sub-cellular fractions and culture media. Both cell lines express 30 kDa (monomeric) galectin-3, although expression was about 15-fold lower in the UMR106 osteosarcoma cells. Dimeric (70 kDa) galectin-3 was additionally observed in the UMR106 cells. Immunofluorescent analysis of galectin-3 distribution showed a diffuse cytoplasmic and strong nuclear pattern in MC3T3E1 osteoblasts, and a patchy cytoplasmic pattern in UMR106 cells. Western blot analysis for both cell lines showed that galectin-3 was mainly found in the cytoplasm and in minor amounts in the microsomal fraction, while considerable amounts were secreted into the culture media. Exposure to 100–200 μg/mL AGEs-BSA increased the cellular content of 30 kDa galectin-3 (20–25% for MC3T3E1 and 35–70% for UMR106 versus control BSA, p < 0.05), and decreased the culture media levels of galectin-3 (10–20% for MC3T3E1 and for UMR106 versus control BSA, p < 0.05). These results confirm the expression of galectin-3 in osteoblastic cells, and suggest different levels and sub-cellular distribution of this protein in transformed versus non-transformed osteoblasts. Osteoblastic exposure to AGEs alters their expression and secretion of galectin-3, which could have significant consequences on osteoblast metabolism and thus on bone turnover.
publishDate 2004
dc.date.none.fl_str_mv 2004
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
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status_str submittedVersion
dc.identifier.none.fl_str_mv https://digital.cic.gba.gob.ar/handle/11746/4949
url https://digital.cic.gba.gob.ar/handle/11746/4949
dc.language.none.fl_str_mv eng
language eng
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http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:CIC Digital (CICBA)
instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron:CICBA
reponame_str CIC Digital (CICBA)
collection CIC Digital (CICBA)
instname_str Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron_str CICBA
institution CICBA
repository.name.fl_str_mv CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
repository.mail.fl_str_mv marisa.degiusti@sedici.unlp.edu.ar
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