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Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses

Bone homeostasis is the equilibrium between organic and inorganic components of the extracellular matrix (ECM) and cells. Alteration of this balance has consequences on bone mass and architecture, resulting in conditions such as osteoporosis (OP). Given ECM protein mutual regulation and their effect...

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Autores principales: Licini, Caterina, Notarstefano, Valentina, Marchi, Saverio, Cerqueni, Giorgia, Ciapetti, Gabriela, Vitale‐Brovarone, Chiara, Giorgini, Elisabetta, Mattioli‐Belmonte, Monica
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9796100/
https://www.ncbi.nlm.nih.gov/pubmed/35661288
http://dx.doi.org/10.1002/biof.1870
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author Licini, Caterina
Notarstefano, Valentina
Marchi, Saverio
Cerqueni, Giorgia
Ciapetti, Gabriela
Vitale‐Brovarone, Chiara
Giorgini, Elisabetta
Mattioli‐Belmonte, Monica
author_facet Licini, Caterina
Notarstefano, Valentina
Marchi, Saverio
Cerqueni, Giorgia
Ciapetti, Gabriela
Vitale‐Brovarone, Chiara
Giorgini, Elisabetta
Mattioli‐Belmonte, Monica
author_sort Licini, Caterina
collection PubMed
description Bone homeostasis is the equilibrium between organic and inorganic components of the extracellular matrix (ECM) and cells. Alteration of this balance has consequences on bone mass and architecture, resulting in conditions such as osteoporosis (OP). Given ECM protein mutual regulation and their effects on bone structure and mineralization, further insight into their expression is crucial to understanding bone biology under normal and pathological conditions. This study focused on Type I Collagen, which is mainly responsible for structural properties and mineralization of bone, and selected proteins implicated in matrix composition, mineral deposition, and cell‐matrix interaction such as Decorin, Osteocalcin, Osteopontin, Bone Sialoprotein 2, Osteonectin and Transforming Growth Factor beta. We developed a novel multidisciplinary approach in order to assess bone matrix in healthy and OP conditions more comprehensively by exploiting the Fourier Transform Infrared Imaging (FTIRI) technique combined with histomorphometry, Sirius Red staining, immunohistochemistry, and Western Blotting. This innovatory procedure allowed for the analysis of superimposed tissue sections and revealed that the alterations in OP bone tissue architecture were associated with warped Type I Collagen structure and deposition but not with changes in the total protein amount. The detected changes in the expression and/or cooperative or antagonist role of Decorin, Osteocalcin, Osteopontin, and Bone Sialoprotein‐2 indicate the deep impact of these NCPs on collagen features of OP bone. Overall, our strategy may represent a starting point for designing targeted clinical strategies aimed at bone mass preservation and sustain the FTIRI translational capability as upcoming support for traditional diagnostic methods.
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spelling pubmed-97961002022-12-28 Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses Licini, Caterina Notarstefano, Valentina Marchi, Saverio Cerqueni, Giorgia Ciapetti, Gabriela Vitale‐Brovarone, Chiara Giorgini, Elisabetta Mattioli‐Belmonte, Monica Biofactors Research Communications Bone homeostasis is the equilibrium between organic and inorganic components of the extracellular matrix (ECM) and cells. Alteration of this balance has consequences on bone mass and architecture, resulting in conditions such as osteoporosis (OP). Given ECM protein mutual regulation and their effects on bone structure and mineralization, further insight into their expression is crucial to understanding bone biology under normal and pathological conditions. This study focused on Type I Collagen, which is mainly responsible for structural properties and mineralization of bone, and selected proteins implicated in matrix composition, mineral deposition, and cell‐matrix interaction such as Decorin, Osteocalcin, Osteopontin, Bone Sialoprotein 2, Osteonectin and Transforming Growth Factor beta. We developed a novel multidisciplinary approach in order to assess bone matrix in healthy and OP conditions more comprehensively by exploiting the Fourier Transform Infrared Imaging (FTIRI) technique combined with histomorphometry, Sirius Red staining, immunohistochemistry, and Western Blotting. This innovatory procedure allowed for the analysis of superimposed tissue sections and revealed that the alterations in OP bone tissue architecture were associated with warped Type I Collagen structure and deposition but not with changes in the total protein amount. The detected changes in the expression and/or cooperative or antagonist role of Decorin, Osteocalcin, Osteopontin, and Bone Sialoprotein‐2 indicate the deep impact of these NCPs on collagen features of OP bone. Overall, our strategy may represent a starting point for designing targeted clinical strategies aimed at bone mass preservation and sustain the FTIRI translational capability as upcoming support for traditional diagnostic methods. John Wiley & Sons, Inc. 2022-06-06 2022 /pmc/articles/PMC9796100/ /pubmed/35661288 http://dx.doi.org/10.1002/biof.1870 Text en © 2022 The Authors. BioFactors published by Wiley Periodicals LLC on behalf of International Union of Biochemistry and Molecular Biology. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Communications
Licini, Caterina
Notarstefano, Valentina
Marchi, Saverio
Cerqueni, Giorgia
Ciapetti, Gabriela
Vitale‐Brovarone, Chiara
Giorgini, Elisabetta
Mattioli‐Belmonte, Monica
Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses
title Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses
title_full Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses
title_fullStr Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses
title_full_unstemmed Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses
title_short Altered type I collagen networking in osteoporotic human femoral head revealed by histomorphometric and Fourier transform infrared imaging correlated analyses
title_sort altered type i collagen networking in osteoporotic human femoral head revealed by histomorphometric and fourier transform infrared imaging correlated analyses
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9796100/
https://www.ncbi.nlm.nih.gov/pubmed/35661288
http://dx.doi.org/10.1002/biof.1870
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