Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix

The adhesion of osteoblasts to bone extracellular matrix, of which type-I collagen constitutes >85%, can modulate diverse aspects of their physiology such as growth, differentiation and mineralisation. In this study we examined the adhesion of UMR106 rat osteoblast-like cells either to a control...

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Autores principales: McCarthy, Antonio Desmond, Uemura, Toshimasa, Etcheverry, Susana Beatriz, Cortizo, Ana María
Formato: Articulo
Lenguaje:Inglés
Publicado: 2004
Materias:
Química
Advanced glycation endproducts
Osteoblast
Adhesion
Integrin receptors
Type-I collagen
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/100327
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-100327
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Advanced glycation endproducts
Osteoblast
Adhesion
Integrin receptors
Type-I collagen
spellingShingle Química
Advanced glycation endproducts
Osteoblast
Adhesion
Integrin receptors
Type-I collagen
McCarthy, Antonio Desmond
Uemura, Toshimasa
Etcheverry, Susana Beatriz
Cortizo, Ana María
Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix
topic_facet Química
Advanced glycation endproducts
Osteoblast
Adhesion
Integrin receptors
Type-I collagen
description The adhesion of osteoblasts to bone extracellular matrix, of which type-I collagen constitutes >85%, can modulate diverse aspects of their physiology such as growth, differentiation and mineralisation. In this study we examined the adhesion of UMR106 rat osteoblast-like cells either to a control (Col) or advanced-glycation-endproduct-modified (AGEs-Col) type I collagen matrix. We investigated the possible role of different integrin receptors in osteoblastic adhesion, by co-incubating these cells either with β-peptide (conserved sequence 113–125 of the β subunit of integrins) or with two other peptides, RGD (Arg-Gly-Asp) and DGEA (Asp-Gly-Glu-Ala), which are recognition sequences for the α-subunits of α1,5β1and α2β1integrins. Collagen glycation inhibited the adhesion of UMR106 osteoblasts to the matrix (40% reduction versus Col,P<0.001). β-Peptide showed a dose- and glycation-dependent inhibitory effect on adhesion, and at a concentration of 100μM decreased the attachment of UMR106 cells to both matrices (42% to Col,P<0.001; and 25% to AGEs-Col,P<0.01). The synthetic peptides RGD (1mM) and DGEA (5mM) inhibited the attachment of UMR106 cells to Col (30 and 20%,P<0.01 andP<0.001, respectively), but not to AGEs-Col. β-Peptide induced an increase in UMR106 cell clumping and a decrease in cellular spreading, while DGEA increased spreading with cellular extensions in multiple directions. These results indicate that both α and β integrin subunits participate in osteoblastic attachment to type-I collagen, probably through the α1,5β1and α2β1integrins. AGEs-modification of type-I collagen impairs the integrin-mediated adhesion of osteoblastic cells to the matrix, and could thus contribute to the pathogenesis of diabetic osteopenia.
format Articulo
Articulo
author McCarthy, Antonio Desmond
Uemura, Toshimasa
Etcheverry, Susana Beatriz
Cortizo, Ana María
author_facet McCarthy, Antonio Desmond
Uemura, Toshimasa
Etcheverry, Susana Beatriz
Cortizo, Ana María
author_sort McCarthy, Antonio Desmond
title Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix
title_short Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix
title_full Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix
title_fullStr Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix
title_full_unstemmed Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix
title_sort advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-i collagen matrix
publishDate 2004
url http://sedici.unlp.edu.ar/handle/10915/100327
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AT etcheverrysusanabeatriz advancedglycationendproductsinterferewithintegrinmediatedosteoblasticattachmenttoatypeicollagenmatrix
AT cortizoanamaria advancedglycationendproductsinterferewithintegrinmediatedosteoblasticattachmenttoatypeicollagenmatrix
bdutipo_str Repositorios
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