Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix
| cic.isFulltext | true | es |
| cic.isPeerReviewed | true | es |
| cic.lugarDesarrollo | Universidad Nacional de La Plata | es |
| cic.version | info:eu-repo/semantics/submittedVersion | es |
| dc.date.accessioned | 2016-12-02T17:24:00Z | |
| dc.date.available | 2016-12-02T17:24:00Z | |
| dc.identifier.uri | https://digital.cic.gba.gob.ar/handle/11746/4897 | |
| dc.title | Advanced glycation endproducts interfere with integrin-mediated osteoblastic attachment to a type-I collagen matrix | en |
| dc.type | Artículo | es |
| dcterms.abstract | 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,<em>P</em><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,<em>P</em><0.001; and 25% to AGEs-Col,<em>P</em><0.01). The synthetic peptides RGD (1mM) and DGEA (5mM) inhibited the attachment of UMR106 cells to Col (30 and 20%,<em>P</em><0.01 and<em>P</em><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. | en |
| dcterms.creator.author | McCarthy, Antonio Desmond | es |
| dcterms.creator.author | Uemurab, Toshimasa | es |
| dcterms.creator.author | Etcheverry, Susana B. | es |
| dcterms.creator.author | Cortizo, Ana María | es |
| dcterms.extent | 9 p. | es |
| dcterms.isPartOf.issue | vol. 36, no. 5 | es |
| dcterms.isPartOf.series | International Journal of Biochemistry and Cell Biology | es |
| dcterms.issued | 2004 | |
| dcterms.language | Inglés | es |
| dcterms.license | Attribution 4.0 International (BY 4.0) | es |
| dcterms.subject | Advanced glycation endproducts | en |
| dcterms.subject | Osteoblast | en |
| dcterms.subject | Adhesion | en |
| dcterms.subject | Integrin receptors | en |
| dcterms.subject | Type-I collagen | en |
| dcterms.subject.materia | Ciencias Químicas | es |
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